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Conserved domains on  [gi|544346093|ref|NP_001269722|]
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filamin A-interacting protein 1-like isoform 4 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
3-348 1.85e-12

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 70.86  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEftlkedltklktltvmfvdERKT 82
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-------------------EKAE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  83 MSEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLkAEEEKGNDLLSRVN 162
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAK 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 163 MLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMK------------TED 230
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEE 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 231 EYETLERRY-------ANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEEEAKSGHLSREvdALKEKIH 303
Cdd:PRK03918 449 HRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAE 525
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 544346093 304 EYMATEDLICHLQGDHSVLQ---KKLNQQENRNRDLGREIENLTKELE 348
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELA 573
 
Name Accession Description Interval E-value
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-348 1.85e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 70.86  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEftlkedltklktltvmfvdERKT 82
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-------------------EKAE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  83 MSEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLkAEEEKGNDLLSRVN 162
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAK 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 163 MLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMK------------TED 230
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEE 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 231 EYETLERRY-------ANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEEEAKSGHLSREvdALKEKIH 303
Cdd:PRK03918 449 HRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAE 525
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 544346093 304 EYMATEDLICHLQGDHSVLQ---KKLNQQENRNRDLGREIENLTKELE 348
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELA 573
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-362 1.07e-11

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: 68.54  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    25 EKERMTTKQLSQELESLKvriKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKlkktEDKLQAASSQLQVE 104
Cdd:TIGR02168  666 AKTNSSILERRREIEELE---EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   105 QNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLK--NK 182
Cdd:TIGR02168  739 EAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAelTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRyanerdkaqfLSKELEHVKMELAK 262
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----------LESELEALLNERAS 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   263 YKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDlicHLQGDHSVLQKKLNQQENRN-RDLGREIE 341
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTlEEAEALEN 961
                          330       340
                   ....*....|....*....|.
gi 544346093   342 NLTKELERYRHFSKSLRPSLN 362
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
32-332 2.78e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  32 KQLSQELESLKV--RIKELEAIESRLEKTEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVT 109
Cdd:COG1196  216 RELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSgk 189
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-- 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 190 sttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKT 269
Cdd:COG1196  373 ------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346093 270 ETSHEQwlfkRLQEEEAKSghLSREVDALKEKIHEYMATEDLICHLQGDHSVLQKKLNQQENR 332
Cdd:COG1196  447 AAEEEA----ELEEEEEAL--LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3-384 1.73e-08

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: 57.81  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKEL----EAIESRLEKTEFTLKEDLTKLKTLTVMFVD 78
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   79 ERKTMSEKLKKTEDKLQAASSQLQV------EQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNK------ 146
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKksseleEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKeqelif 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  147 -LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKStTALHQENNKI----KELSQEVERLKLKLKDMKAI 221
Cdd:pfam05483 444 lLQAREKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKN-IELTAHCDKLllenKELTQEASDMTLELKKHQED 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  222 EDDLMKTED----EYETLERRYANERDKAQFLSKEL----EHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSR 293
Cdd:pfam05483 522 IINCKKQEErmlkQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  294 EVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERyrhFSKSLRPSLNGRRISDPQVFS 373
Cdd:pfam05483 602 QIENKNKNIEELHQENKA---LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEEKLLE 675
                         410
                  ....*....|.
gi 544346093  374 KEVQTEAVDNE 384
Cdd:pfam05483 676 EVEKAKAIADE 686
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
37-214 8.76e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    37 ELESLKV----RIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVT 112
Cdd:smart00787 127 RLEAKKMwyewRMKLLEGLKEGLDENLEGLKEDYKLLM-------KELELLNSIKPKLRDRKDALEEELRQLKQLEDELE 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   113 EKLIEETKRA-LKSKTDVEEKMYSVtKERDDLKNKLKAEEEKGNDLlsrVNMLKNRLQSLEAIEKDFLKNKlnqdsgkst 191
Cdd:smart00787 200 DCDPTELDRAkEKLKKLLQEIMIKV-KKLEELEEELQELESKIEDL---TNKKSELNTEIAEAEKKLEQCR--------- 266
                          170       180
                   ....*....|....*....|...
gi 544346093   192 talHQENNKIKELSQEVERLKLK 214
Cdd:smart00787 267 ---GFTFKEIEKLKEQLKLLQSL 286
 
Name Accession Description Interval E-value
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-348 1.85e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 70.86  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEftlkedltklktltvmfvdERKT 82
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK-------------------EKAE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  83 MSEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLkAEEEKGNDLLSRVN 162
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAK 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 163 MLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMK------------TED 230
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEE 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 231 EYETLERRY-------ANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEEEAKSGHLSREvdALKEKIH 303
Cdd:PRK03918 449 HRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAE 525
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 544346093 304 EYMATEDLICHLQGDHSVLQ---KKLNQQENRNRDLGREIENLTKELE 348
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELA 573
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-362 1.07e-11

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: 68.54  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    25 EKERMTTKQLSQELESLKvriKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKlkktEDKLQAASSQLQVE 104
Cdd:TIGR02168  666 AKTNSSILERRREIEELE---EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL----SRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   105 QNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLK--NK 182
Cdd:TIGR02168  739 EAEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAelTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRyanerdkaqfLSKELEHVKMELAK 262
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----------LESELEALLNERAS 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   263 YKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDlicHLQGDHSVLQKKLNQQENRN-RDLGREIE 341
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTlEEAEALEN 961
                          330       340
                   ....*....|....*....|.
gi 544346093   342 NLTKELERYRHFSKSLRPSLN 362
Cdd:TIGR02168  962 KIEDDEEEARRRLKRLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-349 6.87e-11

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: 65.85  E-value: 6.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    32 KQLSQELESLKVRI---------KELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEkLKKTEDKLQAASSQLQ 102
Cdd:TIGR02168  216 KELKAELRELELALlvlrleelrEELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   103 VEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDflknk 182
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----- 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMkaieddlmktEDEYETLERRYANERDKAQFLSKELEHVKMELAK 262
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERL----------EARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   263 YKLAEKtetshEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLQGdhsvLQKKLNQQENRNRDLGREIEN 342
Cdd:TIGR02168  440 AELEEL-----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA----RLDSLERLQENLEGFSEGVKA 510

                   ....*..
gi 544346093   343 LTKELER 349
Cdd:TIGR02168  511 LLKNQSG 517
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
107-348 7.89e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.47  E-value: 7.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 107 KVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAI-----EKDFLKN 181
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieELEKELE 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 182 KLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEddlmKTEDEYETLERRYANERDKAQFLSKELEHVKMELA 261
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 262 --KYKLAEKTETSheqwlfKRLQEEEAKSGHLSREVDALKEKIHEYmatedlichlqgdHSVLQKKLNQQENRNRDLGRE 339
Cdd:PRK03918 325 giEERIKELEEKE------ERLEELKKKLKELEKRLEELEERHELY-------------EEAKAKKEELERLKKRLTGLT 385

                 ....*....
gi 544346093 340 IENLTKELE 348
Cdd:PRK03918 386 PEKLEKELE 394
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
19-284 2.32e-10

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: 64.32  E-value: 2.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    19 SLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVmfvDERKTMSEKLKKTE---DKLQ 95
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEaeiASLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    96 AASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSL---- 171
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETrdel 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   172 --EAIEKDFLKNKLN----------QDSGKSTTALHQENNKIKELSQEV----ERLKLKLKDMKAIEDDLMKTEDEYETL 235
Cdd:TIGR02169  388 kdYREKLEKLKREINelkreldrlqEELQRLSEELADLNAAIAGIEAKIneleEEKEDKALEIKKQEWKLEQLAADLSKY 467
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 544346093   236 ERRYANERDKAQFLSKELEHVKMELAKyKLAEKTETSHEQWLFKRLQEE 284
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEV 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-343 3.03e-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: 63.92  E-value: 3.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    21 KCNLEKERMTTK--QLSQELESLKvriKELEAIESRLEKTEfTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAAS 98
Cdd:TIGR02168  681 ELEEKIEELEEKiaELEKALAELR---KELEELEEELEQLR-KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    99 SQLQVEQNKVTTVTEKLIEETKRAlksktdvEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDF 178
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEA-------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   179 LKNKlnQDSGKSTTALHQEnnkIKELSQEVERLKLKLKDMKA----IEDDLMKTEDEYETLERRYANERDKAQFLS---K 251
Cdd:TIGR02168  830 ERRI--AATERRLEDLEEQ---IEELSEDIESLAAEIEELEElieeLESELEALLNERASLEEALALLRSELEELSeelR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   252 ELEHVKMELakYKLAEKTETSHEQWlfkRLQEEEAKSghlsrEVDALKEKIHE-YMATEDLIchlQGDHSVLQKKLNQQE 330
Cdd:TIGR02168  905 ELESKRSEL--RRELEELREKLAQL---ELRLEGLEV-----RIDNLQERLSEeYSLTLEEA---EALENKIEDDEEEAR 971
                          330
                   ....*....|...
gi 544346093   331 NRNRDLGREIENL 343
Cdd:TIGR02168  972 RRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3-267 5.19e-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: 63.15  E-value: 5.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKT 82
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    83 MSEKLKKTEDKLQAASSqlqvEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLL---- 158
Cdd:TIGR02168  843 LEEQIEELSEDIESLAA----EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrele 918
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   159 ---SRVNMLKNRLQSLEAiEKDFLKNKLNQDsGKSTTALHQEN-----NKIKELSQEVERLKLKLKDMKAIEddlMKTED 230
Cdd:TIGR02168  919 elrEKLAQLELRLEGLEV-RIDNLQERLSEE-YSLTLEEAEALenkieDDEEEARRRLKRLENKIKELGPVN---LAAIE 993
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 544346093   231 EYETLERRYanerdkaQFLSKELEHVkmELAKYKLAE 267
Cdd:TIGR02168  994 EYEELKERY-------DFLTAQKEDL--TEAKETLEE 1021
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3-305 1.28e-09

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: 61.62  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     3 LEKLEDAFNKSKQEcyslkcnLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLK-TLTVMFVDERK 81
Cdd:TIGR02169  725 IEQLEQEEEKLKER-------LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQ 797
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    82 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV 161
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   162 NMLKNRLQSLEAiEKDFLKNKLNqdsgksttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERR--- 238
Cdd:TIGR02169  878 RDLESRLGDLKK-ERDELEAQLR-----------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdee 945
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093   239 YANERDKAQFLSKELEHVKMELAKYK-LAEKTETSHEQWLfKRLQEEEAKSGHLSREVDALKEKIHEY 305
Cdd:TIGR02169  946 IPEEELSLEDVQAELQRVEEEIRALEpVNMLAIQEYEEVL-KRLDELKEKRAKLEEERKAILERIEEY 1012
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
32-332 2.78e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  32 KQLSQELESLKV--RIKELEAIESRLEKTEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVT 109
Cdd:COG1196  216 RELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSgk 189
Cdd:COG1196  295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-- 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 190 sttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKT 269
Cdd:COG1196  373 ------ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346093 270 ETSHEQwlfkRLQEEEAKSghLSREVDALKEKIHEYMATEDLICHLQGDHSVLQKKLNQQENR 332
Cdd:COG1196  447 AAEEEA----ELEEEEEAL--LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-348 9.87e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 9.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   3 LEKLEDAFNKSKQECYSLKCNLEKERMTtKQLSQELESLKVRIK--ELEAIESRLEKTEFTLKEDLTKLKTLTVMF---- 76
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIgelk 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  77 --VDERKTMSEKLKKTEDKLQAASSQLQVEQNKvtTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEE-- 152
Cdd:PRK03918 419 keIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEli 496
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 153 KGNDLLSRVNMLKNRLQS--LEAIEKDF-----LKNKLNQDSGKSTTaLHQENNKIKELSQEVERLKLKLKDMKAIEDDL 225
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKynLEELEKKAeeyekLKEKLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAEL 575
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 226 MKTEDE-----YETLERR------YANERDKAQFLSKELEHVKMELAKykLAEKTETSheqwlFKRLQEEEAKSGHLSRE 294
Cdd:PRK03918 576 LKELEElgfesVEELEERlkelepFYNEYLELKDAEKELEREEKELKK--LEEELDKA-----FEELAETEKRLEELRKE 648
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 295 VDALKEKI--HEYMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELE 348
Cdd:PRK03918 649 LEELEKKYseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-361 1.39e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERK 81
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  82 TMS-------EKLKKTEDKLQAASSQLQVEQNKVTTVT----------EKLIEETKRAlKSKTDV----------EEKMY 134
Cdd:PRK03918 377 LKKrltgltpEKLEKELEELEKAKEEIEEEISKITARIgelkkeikelKKAIEELKKA-KGKCPVcgrelteehrKELLE 455
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 135 SVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEK-----DFLKN---KLNQDSGKSTTALHQENNKIKE--- 203
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaEQLKEleeKLKKYNLEELEKKAEEYEKLKEkli 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 204 -LSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN-ERDKAQFLSKELEHVKMELakyklaEKTETSHEQWL---- 277
Cdd:PRK03918 536 kLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERL------KELEPFYNEYLelkd 609
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 278 -FKRLQEEEAKSGHLSREVDALKEKIHEymaTEDLICHLQGDHSVLQKKLNQQENRN-----RDLGREIENLTKELERYR 351
Cdd:PRK03918 610 aEKELEREEKELKKLEEELDKAFEELAE---TEKRLEELRKELEELEKKYSEEEYEElreeyLELSRELAGLRAELEELE 686
                        410
                 ....*....|
gi 544346093 352 HFSKSLRPSL 361
Cdd:PRK03918 687 KRREEIKKTL 696
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
121-349 1.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 121 RALKSKTDVEEKMYSVtKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNQDSGKSTTALHQENNK 200
Cdd:COG1196  216 RELKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEEAQAEEYEL 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 201 IKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETsheqwlfKR 280
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-------EA 366
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 281 LQEEEAKSGHLSREVDALKEKIHEymatedlichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLE----------ALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
3-384 1.73e-08

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: 57.81  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKEL----EAIESRLEKTEFTLKEDLTKLKTLTVMFVD 78
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   79 ERKTMSEKLKKTEDKLQAASSQLQV------EQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNK------ 146
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKksseleEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKeqelif 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  147 -LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKStTALHQENNKI----KELSQEVERLKLKLKDMKAI 221
Cdd:pfam05483 444 lLQAREKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKN-IELTAHCDKLllenKELTQEASDMTLELKKHQED 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  222 EDDLMKTED----EYETLERRYANERDKAQFLSKEL----EHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSR 293
Cdd:pfam05483 522 IINCKKQEErmlkQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  294 EVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERyrhFSKSLRPSLNGRRISDPQVFS 373
Cdd:pfam05483 602 QIENKNKNIEELHQENKA---LKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEEKLLE 675
                         410
                  ....*....|.
gi 544346093  374 KEVQTEAVDNE 384
Cdd:pfam05483 676 EVEKAKAIADE 686
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
2-254 2.39e-08

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 57.24  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKqecyslkcnLEKERMTTKQLSQELESLKVRIKELEAIESRLEKteftLKEDLTKLKtltvmfvDERK 81
Cdd:PRK05771  58 ALDKLRSYLPKLN---------PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKE----LEEEISELE-------NEIK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  82 TMSEKLKKTEdKLQAASSQLQVEQN-KVTTVTEKLIEETKralksktdveekmYSVTKERDDLKNKLKAEEEKGNDLLSR 160
Cdd:PRK05771 118 ELEQEIERLE-PWGNFDLDLSLLLGfKYVSVFVGTVPEDK-------------LEELKLESDVENVEYISTDKGYVYVVV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 161 VNmLKNRLQSLEAI--EKDFLKNKLNqDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYetlerr 238
Cdd:PRK05771 184 VV-LKELSDEVEEElkKLGFERLELE-EEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY------ 255
                        250
                 ....*....|....*.
gi 544346093 239 YANERDKAQFLSKELE 254
Cdd:PRK05771 256 LEIELERAEALSKFLK 271
PTZ00121 PTZ00121
MAEBL; Provisional
4-375 2.51e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    4 EKLEDAFNKSKQEcyslKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvDERKTM 83
Cdd:PTZ00121 1377 KKKADAAKKKAEE----KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA------EEAKKA 1446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   84 SEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  164 LKNRLQSLEAIEKDFLKNKLNQDSGKSTTALH--QENNKIKELSQEVERLKLKLK---DMKAIE----DDLMKTEDEYET 234
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRkaeEAKKAEeariEEVMKLYEEEKK 1606
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  235 LE----RRYANERDKAQFLSKElEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATED 310
Cdd:PTZ00121 1607 MKaeeaKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346093  311 lichlqgdhsvLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQVFSKE 375
Cdd:PTZ00121 1686 -----------DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
PTZ00121 PTZ00121
MAEBL; Provisional
4-348 3.02e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKvriKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTM 83
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   84 SEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKmysvtKERDDLKNklKAEEEKGNDLLSRVNM 163
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA-----KKADEAKK--KAEEAKKAEEAKKKAE 1467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  164 LKNRLQSL-----EAIEKDFLKNKLNQDSGKSTTALHQENNKIK-------ELSQEVERLKLKLKDMKAIE----DDLMK 227
Cdd:PTZ00121 1468 EAKKADEAkkkaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeakkaEEAKKADEAKKAEEAKKADEakkaEEKKK 1547
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  228 TEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMA 307
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 544346093  308 TEDlichlqgdhsvLQKKLNQQENRNRDLGREIENLTKELE 348
Cdd:PTZ00121 1628 AEE-----------EKKKVEQLKKKEAEEKKKAEELKKAEE 1657
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
47-343 3.72e-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: 57.00  E-value: 3.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    47 ELEAIESRLEKTEFTLKEDLTKLKTLTvmfvDERKTmSEKLKKTEDKLQAASSQLQVEQNKVTtvtEKLIEETKRALKSK 126
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERLR----REREK-AERYQALLKEKREYEGYELLKEKEAL---ERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   127 TDVEEKmysVTKERDDLKNKLKAEEEKGNDLLSRVNmlknRLQSLEAIEkdfLKNKLnqdsGKSTTALHQENNKIKELSQ 206
Cdd:TIGR02169  250 EEELEK---LTEEISELEKRLEEIEQLLEELNKKIK----DLGEEEQLR---VKEKI----GELEAEIASLERSIAEKER 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   207 EVERLKLKLKDmkaIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKyklaektetsheqwLFKRLQEEEA 286
Cdd:TIGR02169  316 ELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED--------------LRAELEEVDK 378
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 544346093   287 KSGHLSREVDALKEKIHEYmatEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENL 343
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKL---KREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
32-262 4.49e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 55.93  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  32 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTV 111
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-------RRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 112 TEKLiEETKRALKSKTDVEEKMysvtKERDDLKNKLKAEEekGNDLLSRVNMLK----NRLQSLEAIEKDflKNKLNQds 187
Cdd:COG4942   96 RAEL-EAQKEELAELLRALYRL----GRQPPLALLLSPED--FLDAVRRLQYLKylapARREQAEELRAD--LAELAA-- 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 188 gkSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKT-EDEYETLERRYANERDKAQFLSKELEHVKMELAK 262
Cdd:COG4942  165 --LRAELEAERAELEALLAELEEERAALEALKAERQKLLARlEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
PRK01156 PRK01156
chromosome segregation protein; Provisional
3-391 5.00e-08

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 56.45  E-value: 5.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   3 LEKLEDAFNKSKQECYSLKCNLE-----KERMTTKQLsqELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFV 77
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISnidylEEKLKSSNL--ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  78 DERKTMS---EKLKKTEDKLQAASSQLQVEQNKVTTVTEklieetkralksktdVEEKMYSVTKerddlkNKLKAEEEKG 154
Cdd:PRK01156 239 SALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKE---------------LEERHMKIIN------DPVYKNRNYI 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 155 NDLLSRVNMLKNRLQSLEAIEKDFLKNklnQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYET 234
Cdd:PRK01156 298 NDYFKYKNDIENKKQILSNIDAEINKY---HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIES 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 235 LERRYANERDKAQFLSKELEHVkmeLAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEK---IHEYMA---- 307
Cdd:PRK01156 375 LKKKIEEYSKNIERMSAFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENldeLSRNMEmlng 451
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 308 ---------------TEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER-----------YRHFSKSLRPSL 361
Cdd:PRK01156 452 qsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYleseeinksinEYNKIESARADL 531
                        410       420       430
                 ....*....|....*....|....*....|
gi 544346093 362 NGRRISDPQVFSKEVQTEAVDNEppdYKSL 391
Cdd:PRK01156 532 EDIKIKINELKDKHDKYEEIKNR---YKSL 558
PTZ00121 PTZ00121
MAEBL; Provisional
79-304 1.20e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   79 ERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKlIEETKRALKSKTDVEEkmysVTKERDDLKNKlkAEEEKGNDLL 158
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEE----AKKKADAAKKK--AEEAKKAAEA 1347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  159 SRVNMlKNRLQSLEAIEKDFLKNKLNQDSGKSTTalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLE-- 236
Cdd:PTZ00121 1348 AKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKA---DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADea 1423
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346093  237 RRYANERDKAQFLSKELEHV-KMELAKYKLAE--KTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHE 304
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAkKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-355 1.23e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.07  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  23 NLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLtvmfVDERKTMSEKLKKTEDKLQAASSQLQ 102
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEV----LREINEISSELPELREELEKLEKEVK 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 103 vEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKgndlLSRVNMLKNRLQSLEAIEKdfLKNK 182
Cdd:PRK03918 232 -ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK----VKELKELKEKAEEYIKLSE--FYEE 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 183 LNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRyANERDKAQFLSKELEHVKMELA- 261
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTg 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 262 --------KYKLAEKTETSHEqwlfKRLQEEEAKSGHLSREVDALKEKIHEYMAT----------------EDLICHLQG 317
Cdd:PRK03918 384 ltpeklekELEELEKAKEEIE----EEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrKELLEEYTA 459
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 544346093 318 DHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSK 355
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK 497
PTZ00121 PTZ00121
MAEBL; Provisional
25-310 4.03e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   25 EKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVE 104
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  105 QNKVTT-VTEKLIEETKRALKSKTDVEEKmysVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQslEAIEKDFLKNKL 183
Cdd:PTZ00121 1326 EAKKKAdAAKKKAEEAKKAAEAAKAEAEA---AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKKA 1400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  184 NQDSGKSttalhQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLE-RRYANERDKAQFLSKELEHVKMELAK 262
Cdd:PTZ00121 1401 EEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEA 1475
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 544346093  263 YKLAEKTETSHEqwlFKRLQEEEAKSGHLSREVDALKEKIHEYMATED 310
Cdd:PTZ00121 1476 KKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
157-363 4.12e-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: 4.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   157 LLSRVNMLKNRLQSLEaIEKDFLKNKLNqdsgksttalHQENnKIKELSQEVERLKLKLKDmkaIEDDLMKTEDEYETLE 236
Cdd:TIGR02169  672 EPAELQRLRERLEGLK-RELSSLQSELR----------RIEN-RLDELSQELSDASRKIGE---IEKEIEQLEQEEEKLK 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   237 RRYANERDKAQFLSKELEHVKMELAKY--KLAEKTETSHEqwLFKRLQEEEAK-SGHLSREVDALKEKIHEYMA------ 307
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSELKELeaRIEELEEDLHK--LEEALNDLEARlSHSRIPEIQAELSKLEEEVSriearl 814
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093   308 --TEDLICHLQGDHSVLQKKLNQQENRNRDL-------GREIENLTK-------ELERYRHFSKSLRPSLNG 363
Cdd:TIGR02169  815 reIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiksiEKEIENLNGkkeeleeELEELEAALRDLESRLGD 886
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-286 5.57e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 5.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  91 EDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQS 170
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 171 LEAI-EKDFLKNKLNQDSGKsTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMK-----TEDEYETLERRYANERD 244
Cdd:COG4717  128 LPLYqELEALEAELAELPER-LEELEERLEELRELEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQ 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 544346093 245 KAQFLSKELEHVKMEL--AKYKLAEKTETSHEQWLFKRLQEEEA 286
Cdd:COG4717  207 RLAELEEELEEAQEELeeLEEELEQLENELEAAALEERLKEARL 250
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2-358 7.32e-07

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: 52.67  E-value: 7.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERK 81
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    82 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKtdvEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV 161
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL---KSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   162 NMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKElsqevERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN 241
Cdd:pfam02463  331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE-----EELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   242 ERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKR--------LQEEEAKSGHLSREVDALKEKIHEYMATEDLIC 313
Cdd:pfam02463  406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 544346093   314 HLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLR 358
Cdd:pfam02463  486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
168-351 8.94e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 168 LQSLEAIEKDFLKNKLNQ---DSGKSTTALHQEnnkIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERD 244
Cdd:COG4717   40 LAFIRAMLLERLEKEADElfkPQGRKPELNLKE---LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 245 KAQFLSKELEHVKMELAKYKLAEKTETSHEQWlfKRLQEEEAKSGHLSREVDALKEKIHEY------------MATEDLI 312
Cdd:COG4717  117 ELEKLEKLLQLLPLYQELEALEAELAELPERL--EELEERLEELRELEEELEELEAELAELqeeleelleqlsLATEEEL 194
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 544346093 313 CHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYR 351
Cdd:COG4717  195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
30-261 1.55e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  30 TTKQLSQELESLKvriKELEAIESRLEktEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVT 109
Cdd:COG3206  176 ALEFLEEQLPELR---KELEEAEAALE--EFRQKNGLVDLS-------EEAKLLLQQLSELESQLAEARAELAEAEARLA 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLieETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiekdflknKLNQDSGK 189
Cdd:COG3206  244 ALRAQL--GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--------QLQQEAQR 313
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093 190 STTALHQEnnkIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA 261
Cdd:COG3206  314 ILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
COG5022 COG5022
Myosin heavy chain [General function prediction only];
11-413 2.06e-06

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 51.23  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   11 NKSKQECYS-LKCNLEKeRMTTKQLSQELESLKVRIKELEAiESRLEKTEFTLkEDLTKLKTLTVmfvDERKTMSEKLKK 89
Cdd:COG5022   923 LEFKTELIArLKKLLNN-IDLEEGPSIEYVKLPELNKLHEV-ESKLKETSEEY-EDLLKKSTILV---REGNKANSELKN 996
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   90 TEDKLQAASSQLQVEQNKVttvteKLIEETKRALKSKTDVEEKMYSVTKErddLKNKLKAEEEKGNDLLSrVNMLKNRLQ 169
Cdd:COG5022   997 FKKELAELSKQYGALQEST-----KQLKELPVEVAELQSASKIISSESTE---LSILKPLQKLKGLLLLE-NNQLQARYK 1067
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  170 SLEaIEKDFLKNKLNQDSGKSTTalhqeNNKIKElsqeverlkLKLKDMKAIEDDLMKTEDEYETL---ERRYANERDKA 246
Cdd:COG5022  1068 ALK-LRRENSLLDDKQLYQLEST-----ENLLKT---------INVKDLEVTNRNLVKPANVLQFIvaqMIKLNLLQEIS 1132
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  247 QFLSKELEHVKMELAKYKLAEKT-----------ETSHEQWlFKRLQEEEAKSGH---------------LSREVDALKE 300
Cdd:COG5022  1133 KFLSQLVNTLEPVFQKLSVLQLEldglfweanleALPSPPP-FAALSEKRLYQSAlydeksklsssevndLKNELIALFS 1211
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  301 KIHEYMATEDLICHL--QGDHSVLQKKLNQQENRNRDLGREIENLTKelERYRHFSKSLRPSLNGRRISdPQVFSKEVQT 378
Cdd:COG5022  1212 KIFSGWPRGDKLKKLisEGWVPTEYSTSLKGFNNLNKKFDTPASMSN--EKLLSLLNSIDNLLSSYKLE-EEVLPATINS 1288
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 544346093  379 EAVDNEPPDYKSLIPLERAVINGQLYEESENQDED 413
Cdd:COG5022  1289 LLQYINVGLFNALRTKASSLRWKSATEVNYNSEEL 1323
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-284 2.07e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   3 LEKLEDAFNKSKQECYSLKCNLEKER--MTTKQLSQELESLKVRIKELEAIESRLEKTEF-TLKEDLTKLKTLTVMFVDE 79
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAEEYeKLKEKLIKLKGEIKSLKKE 547
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  80 RKTMSE---KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALK----------SKTDVEEKMYSVTKERDDLKNK 146
Cdd:PRK03918 548 LEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKelepfyneylELKDAEKELEREEKELKKLEEE 627
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 147 LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLM 226
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 227 KTEDEYETLERryanERDKAQFLSKELEHVKMELAKYKLAEKTETSHEqwLFKRLQEE 284
Cdd:PRK03918 708 KAKKELEKLEK----ALERVEELREKVKKYKALLKERALSKVGEIASE--IFEELTEG 759
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
25-384 3.77e-06

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: 50.49  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   25 EKERMTTKQLSQELESLKVRIKELEAIESRLEK---TEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEdklqaASSQL 101
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmsTQKALEEDLQIATKTICQLTEEKEAQMEELNKAK-----AAHSF 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  102 QVEQNKVTTVTeklIEETKRALKSKTDveekmysvtKERDDLKnKLKAEEEKGNDLLSRVNMLKNRlqslEAIEKDFLKN 181
Cdd:pfam05483 350 VVTEFEATTCS---LEELLRTEQQRLE---------KNEDQLK-IITMELQKKSSELEEMTKFKNN----KEVELEELKK 412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  182 KLNQDSgksttALHQENNKIKELSQEVERLKLKLKDMkaieddLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA 261
Cdd:pfam05483 413 ILAEDE-----KLLDEKKQFEKIAEELKGKEQELIFL------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  262 KYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichlqgdhsvLQKKLNQQENRNRDLGREIE 341
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER----------MLKQIENLEEKEMNLRDELE 551
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 544346093  342 NLTKELERYRHFSK-SLRPSLNGRRISDPQVFSKEVQTEAVDNE 384
Cdd:pfam05483 552 SVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENK 595
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
4-353 9.06e-06

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: 49.45  E-value: 9.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQL---SQELESLKVRIKELEAIESRLEKTeFTLKEDLTklktltvmfvDER 80
Cdd:pfam12128  426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA-NAEVERLQ----------SEL 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    81 KTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRAL----KSKTDVEEKMYSVTKE----RDDLKNKLKAEEE 152
Cdd:pfam12128  495 RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLhflrKEAPDWEQSIGKVISPellhRTDLDPEVWDGSV 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   153 KGNDLLSRVNMlknRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQ-------EVERLKLKLKDMKAI---- 221
Cdd:pfam12128  575 GGELNLYGVKL---DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEqlvqangELEKASREETFARTAlkna 651
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   222 EDDLMKTEDEYETLERR----YANERDKAQFLSKELEHVKMELA---KYKLAEKTETSHE---QWLFKRLQEEEAKSGHL 291
Cdd:pfam12128  652 RLDLRRLFDEKQSEKDKknkaLAERKDSANERLNSLEAQLKQLDkkhQAWLEEQKEQKREartEKQAYWQVVEGALDAQL 731
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093   292 SReVDALKEKIHEYMATEDLICHLQGDHSVlqKKLNQQENRNRDLGREIENLTKELERYRHF 353
Cdd:pfam12128  732 AL-LKAAIAARRSGAKAELKALETWYKRDL--ASLGVDPDVIAKLKREIRTLERKIERIAVR 790
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1-347 1.08e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.96  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     1 MALEKLEDAFNKSKQECYSL-----------KCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKE----- 64
Cdd:pfam15921  426 MEVQRLEALLKAMKSECQGQmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDltasl 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    65 ------------DLTKLKTLtvmfVDERKTMSEKLKKTEDKLQAASSQLQ------VEQNKVTTVTEKLIEETKRAL--- 123
Cdd:pfam15921  506 qekeraieatnaEITKLRSR----VDLKLQELQHLKNEGDHLRNVQTECEalklqmAEKDKVIEILRQQIENMTQLVgqh 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   124 -KSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEaIEKDFLKNklnqdsgksttALHQENNKIK 202
Cdd:pfam15921  582 gRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVN-----------AGSERLRAVK 649
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   203 ELSQEVERLklkLKDMKAIEDDLMKTEDEYETLERRYANErdkaqflSKELEhvkMELAKYKLAEKTETSHEQWLFKRLQ 282
Cdd:pfam15921  650 DIKQERDQL---LNEVKTSRNELNSLSEDYEVLKRNFRNK-------SEEME---TTTNKLKMQLKSAQSELEQTRNTLK 716
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346093   283 EEEAKSGHLSREVDALKEKIheyMATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 347
Cdd:pfam15921  717 SMEGSDGHAMKVAMGMQKQI---TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
112-351 1.24e-05

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: 48.90  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   112 TEKLIEETKRALksktdveEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKL---NQDSG 188
Cdd:TIGR02168  177 TERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELeelQEELK 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   189 KSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYanERDKaQFLSKELEHVKMELAKYKLAEK 268
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQK-QILRERLANLERQLEELEAQLE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   269 TETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMAT-EDLICHLQGdhsvLQKKLNQQENRNRDLGREIENLTKEL 347
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAElEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEI 402

                   ....
gi 544346093   348 ERYR 351
Cdd:TIGR02168  403 ERLE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-233 1.37e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKQECYSLK---------CNLEKERMttKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTl 72
Cdd:COG1196  275 ELEELELELEEAQAEEYELLaelarleqdIARLEERR--RELEERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  73 tvmfvdERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMysvTKERDDLKNKLKAEEE 152
Cdd:COG1196  352 ------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---EAEEALLERLERLEEE 422
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 153 KGNDLLSRVNMLKNRLQSLEAIEKDFLK-NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDE 231
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEeAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502

                 ..
gi 544346093 232 YE 233
Cdd:COG1196  503 YE 504
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
4-357 1.48e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.63  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLkvrikELE-AIESRLEKTEFTLKEDLTKLKTLTVMFVD---- 78
Cdd:pfam01576  243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDL-----ESErAARNKAEKQRRDLGEELEALKTELEDTLDttaa 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    79 ------ERKTMSEKLKKT-EDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEE 151
Cdd:pfam01576  318 qqelrsKREQEVTELKKAlEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQ 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   152 EKGNDLLSRVNMLKNRLQSLEA--IEKDFLKNKLNQDSGKS-------TTALHQENNKIKELSQEVERLKLKLKDMK--- 219
Cdd:pfam01576  398 QAKQDSEHKRKKLEGQLQELQArlSESERQRAELAEKLSKLqselesvSSLLNEAEGKNIKLSKDVSSLESQLQDTQell 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   220 --------AIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELA--KYKLAEKTETSHeqwlfkrlQEEEAKSg 289
Cdd:pfam01576  478 qeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmKKKLEEDAGTLE--------ALEEGKK- 548
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093   290 HLSREVDALKEKIHEYMATEDlichlqgdhsvlqkKLNQQENRnrdLGREIENLTKELERYRHFSKSL 357
Cdd:pfam01576  549 RLQRELEALTQQLEEKAAAYD--------------KLEKTKNR---LQQELDDLLVDLDHQRQLVSNL 599
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-349 1.92e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  32 KQLSQELESLKVRIKELEAIESRLEK-------------TEFTLKEDLTKLKTLTVMfVDERKTMSEKLKKTEDKLQAAS 98
Cdd:COG4717   98 EELEEELEELEAELEELREELEKLEKllqllplyqeleaLEAELAELPERLEELEER-LEELRELEEELEELEAELAELQ 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  99 SQLQVEQNKVTTVTEKLIEETKRALKS-----------KTDVEEKMYSVTKERDDLKNKLKAEEEK-------------- 153
Cdd:COG4717  177 EELEELLEQLSLATEEELQDLAEELEElqqrlaeleeeLEEAQEELEELEEELEQLENELEAAALEerlkearlllliaa 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 154 --------GNDLLSRVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMK 219
Cdd:COG4717  257 allallglGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 220 AIEDDLMKTEDEYETLERRYANERDKAQFlsKELEHVKMELAKYKLAEkTETSHEQWL--FKRLQEEEAKSGHLSREVDA 297
Cdd:COG4717  337 EELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEEYQELKEELEELEEQLEE 413
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544346093 298 LKEKIHEYMATEDLIcHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:COG4717  414 LLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAELEAELEQ 464
PTZ00121 PTZ00121
MAEBL; Provisional
55-300 2.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   55 LEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMY 134
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  135 SVTKERDDLKNKLKaEEEKGNDLLSRVNMLKNRLQSLEAIEKDflKNKLNQDSGKSTTALHQENNKIK-ELSQEVERLKL 213
Cdd:PTZ00121 1375 EAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKAAAA--KKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKK 1451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  214 KLKDMKAIEDDLMKTEDEYETLE-RRYANERDKAQFLSKELEHV--KMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGH 290
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEEAkkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
                         250
                  ....*....|
gi 544346093  291 LSREVDALKE 300
Cdd:PTZ00121 1532 EAKKADEAKK 1541
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-349 2.14e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKvRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMfVDERK 81
Cdd:COG4717   82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEER-LEELR 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  82 TMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKS-----------KTDVEEKMYSVTKERDDLKNKLKAE 150
Cdd:COG4717  160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqrlaeleeeLEEAQEELEELEEELEQLENELEAA 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 151 EEK----------------------GNDLLSRVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIK 202
Cdd:COG4717  240 ALEerlkearlllliaaallallglGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQALPALEELEEE 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 203 ELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFlsKELEHVKMELAKYKLAEkTETSHEQWL--FKR 280
Cdd:COG4717  320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELEQEIAALLAEAGVE-DEEELRAALeqAEE 396
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093 281 LQEEEAKSGHLSREVDALKEKIHEYMATEDLichlqgdhSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:COG4717  397 YQELKEELEELEEQLEELLGELEELLEALDE--------EELEEELEELEEELEELEEELEELREELAE 457
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
3-348 3.64e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    3 LEKLEDAFNKSKQECYSLKCNLEKERmttKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTvmfvderkT 82
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENEL---NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE--------S 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   83 MSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN 162
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  163 MLKN-RLQSLEAIEKDFLKNKLNQDSgKSTTALHQENNKIKELSQEVERLKLKLKDM----KAIEDDLMKTEDEYETLER 237
Cdd:TIGR04523 299 DLNNqKEQDWNKELKSELKNQEKKLE-EIQNQISQNNKIISQLNEQISQLKKELTNSesenSEKQRELEEKQNEIEKLKK 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  238 RYANERDKAQFLSKELEHVKMELAKYKLAE-------KTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHE----YM 306
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVkeliIK 457
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 544346093  307 ATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELE 348
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
54-368 3.95e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 47.35  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    54 RLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKM 133
Cdd:TIGR00606  685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   134 YSVTKERDDLKNkLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKE-------LSQ 206
Cdd:TIGR00606  765 NDIEEQETLLGT-IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEkqheldtVVS 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   207 EVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMEL----AKYKLAEKTETSHEQWLFKRLQ 282
Cdd:TIGR00606  844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQDSPLETFLEKDQQ 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   283 EEEA--KSGHLSR-----EVDALKEK---IHEYMatEDLICHLQGDHsvlQKKLNQQENRNRDLGREIENLTKELERYRH 352
Cdd:TIGR00606  924 EKEEliSSKETSNkkaqdKVNDIKEKvknIHGYM--KDIENKIQDGK---DDYLKQKETELNTVNAQLEECEKHQEKINE 998
                          330
                   ....*....|....*.
gi 544346093   353 FSKSLRPSLNGRRISD 368
Cdd:TIGR00606  999 DMRLMRQDIDTQKIQE 1014
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
21-386 4.26e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 47.04  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    21 KCNLEKERMTTKQLSQELESLK----VRIKELEAIESRLEKTEFTL----KEDLTKLKTLTvmfvDERKTMSEKLKKTED 92
Cdd:pfam15921  592 KAQLEKEINDRRLELQEFKILKdkkdAKIRELEARVSDLELEKVKLvnagSERLRAVKDIK----QERDQLLNEVKTSRN 667
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    93 KLQAASSQLQVEQNKVTTVTEKLiEETKRALKSKtdveekMYSVTKERDDLKNKLKAEEEKGNDLLS------------- 159
Cdd:pfam15921  668 ELNSLSEDYEVLKRNFRNKSEEM-ETTTNKLKMQ------LKSAQSELEQTRNTLKSMEGSDGHAMKvamgmqkqitakr 740
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   160 -RVNMLKNRLQSLEAI------EKDFLKNKLNQDSGKSTTALHQENNKIKEL----SQEvERLKLKLKDMKAIEDDLMKT 228
Cdd:pfam15921  741 gQIDALQSKIQFLEEAmtnankEKHFLKEEKNKLSQELSTVATEKNKMAGELevlrSQE-RRLKEKVANMEVALDKASLQ 819
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   229 EDEYETLERRYANE--RDKAQFL--SKELE---HVKMELAKYKLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKEK 301
Cdd:pfam15921  820 FAECQDIIQRQEQEsvRLKLQHTldVKELQgpgYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKED 899
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   302 iheymATEDLICHLQGDHSVLQKKLNQQENRNRDLGRE---------IENLTKELERYRHFSKSLRPSLNGRRISDPQVF 372
Cdd:pfam15921  900 -----PTRDLKQLLQELRSVINEEPTVQLSKAEDKGRApslgalddrVRDCIIESSLRSDICHSSSNSLQTEGSKSSETC 974
                          410
                   ....*....|....*
gi 544346093   373 SKE-VQTEAVDNEPP 386
Cdd:pfam15921  975 SREpVLLHAGELEDP 989
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
91-348 5.60e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 5.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    91 EDKLQAASSQLQVEQNKVTTVTEKLieetkralkskTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQS 170
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESEL-----------KELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   171 LEAIEKDfLKNKLNQDSGKStTALHQENNKIKELSQEVE---------RLKLKLK------DMKAIEDDLMKTED----- 230
Cdd:pfam01576   73 LEEILHE-LESRLEEEEERS-QQLQNEKKKMQQHIQDLEeqldeeeaaRQKLQLEkvtteaKIKKLEEDILLLEDqnskl 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   231 --EYETLERR-------YANERDKAQFLSK----------ELE---------HVKMELAKYKLAEKTETSHEQWLFKRLQ 282
Cdd:pfam01576  151 skERKLLEERiseftsnLAEEEEKAKSLSKlknkheamisDLEerlkkeekgRQELEKAKRKLEGESTDLQEQIAELQAQ 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   283 EEEAKsGHLSR---EVDALKEKIHEYMATEDL----ICHLQGDHSVLQKKL-------NQQENRNRDLGREIENLTKELE 348
Cdd:pfam01576  231 IAELR-AQLAKkeeELQAALARLEEETAQKNNalkkIRELEAQISELQEDLeseraarNKAEKQRRDLGEELEALKTELE 309
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
32-357 5.62e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 46.50  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    32 KQLSQELESLKVRIKELEAIESRLEKTEFTL-------KEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVE 104
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   105 QNKV-TTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIekdflKNKL 183
Cdd:TIGR00618  625 QDLQdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW-----KEML 699
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   184 NQdsgkSTTALHQENNKIKELSQEVERLKLKLKDMKAiedDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKY 263
Cdd:TIGR00618  700 AQ----CQTLLRELETHIEEYDREFNEIENASSSLGS---DLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA 772
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   264 KLAEKTETSH-EQWLFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLICHLqgdhsvLQKKLNQQENRNRDLGREIEN 342
Cdd:TIGR00618  773 ALQTGAELSHlAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET------LVQEEEQFLSRLEEKSATLGE 846
                          330
                   ....*....|....*
gi 544346093   343 LTKELERYRHFSKSL 357
Cdd:TIGR00618  847 ITHQLLKYEECSKQL 861
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
111-312 8.38e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 111 VTEKLIEEtkralksKTDVEEKMYSVTKERDDlkNKLKAEEEKGNDLLSRVNMLKNRLQSLEaiekdflknklnqdsgks 190
Cdd:COG2433  381 ALEELIEK-------ELPEEEPEAEREKEHEE--RELTEEEEEIRRLEEQVERLEAEVEELE------------------ 433
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 191 ttalhqenNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANerdkaqfLSKELEHVKMELAkyKLAEKTE 270
Cdd:COG2433  434 --------AELEEKDERIERLERELSEARSEERREIRKDREISRLDREIER-------LERELEEERERIE--ELKRKLE 496
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544346093 271 tsheqwLFKRLQEEEAKSGHLSREV------DALKEKIHEY-MATEDLI 312
Cdd:COG2433  497 ------RLKELWKLEHSGELVPVKVvekftkEAIRRLEEEYgLKEGDVV 539
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
110-351 9.26e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 9.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 110 TVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiekdfLKNKLNQDSGK 189
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELRE-----KRDELNEKVKE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 190 STTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRY-------ANER---DKAQFLSKELEHVKME 259
Cdd:COG1340   76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqtevlspEEEKelvEKIKELEKELEKAKKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 260 LAKYKLAEKTETSHEQW------LFKRLQEEEAKSGHLSREVDALKEKIHEYMATEDLichLQGDHSVLQKKLNQQENRN 333
Cdd:COG1340  156 LEKNEKLKELRAELKELrkeaeeIHKKIKELAEEAQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADELHEEI 232
                        250
                 ....*....|....*...
gi 544346093 334 RDLGREIENLTKELERYR 351
Cdd:COG1340  233 IELQKELRELRKELKKLR 250
PTZ00121 PTZ00121
MAEBL; Provisional
4-347 1.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    4 EKLEDAFNKS--KQECYSLKCNLEKERmTTKQLSQELESLKVRIKELEAIESRLEKTEfTLKEDLTKLKTLTVMFVDERK 81
Cdd:PTZ00121 1457 KKAEEAKKKAeeAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAK 1534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   82 TmSEKLKKTEDKLQAASSQLQVEQNKVTTVteKLIEETKRALKSKT----------DVEEKMYSVTKERDDLKNKLKAEE 151
Cdd:PTZ00121 1535 K-ADEAKKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDKNmalrkaeeakKAEEARIEEVMKLYEEEKKMKAEE 1611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  152 EKGNDLlSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALH-QENNKIK--ELSQEVERLKLKLKDMKAIEDDLMKT 228
Cdd:PTZ00121 1612 AKKAEE-AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaEEENKIKaaEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  229 EDEYetleRRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLfKRLQEEEAKSGHLSREVDALKEKIHEYMAT 308
Cdd:PTZ00121 1691 AEAL----KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA-KKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 544346093  309 EDLICH--LQGDHSVLQKKLNQQENRNRdlgREIENLTKEL 347
Cdd:PTZ00121 1766 EEKKAEeiRKEKEAVIEEELDEEDEKRR---MEVDKKIKDI 1803
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
34-277 1.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  34 LSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKL---KTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQnkvtt 110
Cdd:COG4717  293 LAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEE----- 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 111 vteklIEETKRALKSKTDVEEkmysvtkeRDDLKNKLKAEEEKgNDLLSRVNMLKNRLQSL----EAIEKDFLKNKLNQD 186
Cdd:COG4717  368 -----LEQEIAALLAEAGVED--------EEELRAALEQAEEY-QELKEELEELEEQLEELlgelEELLEALDEEELEEE 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 187 SGKSTTALHQENNKIKELSQEVERLKLKLKDMKAiEDDLMKTEDEYETLerryanerdKAQFLSKELEHVKMELAKYKLA 266
Cdd:COG4717  434 LEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEEL---------KAELRELAEEWAALKLALELLE 503
                        250
                 ....*....|.
gi 544346093 267 EKTETSHEQWL 277
Cdd:COG4717  504 EAREEYREERL 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-412 1.76e-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: 45.06  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRL--EKTEFT-----LKEDLTKLKTLTV 74
Cdd:TIGR02169  358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeELQRLSeeladLNAAIAGIEAKIN 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    75 MFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLieetkralkskTDVEEKMYSVTKERDDLKNKLKAEEEKG 154
Cdd:TIGR02169  438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-----------DRVEKELSKLQRELAEAEAQARASEERV 506
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   155 NDLLSRVNMLKNRLQ------------------SLEAIEKDFLKNKLNQDSGKSTTA---LHQEN---------NKIKEL 204
Cdd:TIGR02169  507 RGGRAVEEVLKASIQgvhgtvaqlgsvgeryatAIEVAAGNRLNNVVVEDDAVAKEAielLKRRKagratflplNKMRDE 586
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   205 SQEVERLKLKLKDMKAIedDLMKTEDEYE-----------------------------TLE------------------- 236
Cdd:TIGR02169  587 RRDLSILSEDGVIGFAV--DLVEFDPKYEpafkyvfgdtlvvedieaarrlmgkyrmvTLEgelfeksgamtggsraprg 664
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   237 --RRYANERDKAQFLSKELEHVKMELA--KYKLAEKTETSHEqwLFKRLQEEEAKSGHLSREVDALKEKIHeymATEDLI 312
Cdd:TIGR02169  665 giLFSRSEPAELQRLRERLEGLKRELSslQSELRRIENRLDE--LSQELSDASRKIGEIEKEIEQLEQEEE---KLKERL 739
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   313 CHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQVFSKEVQTEAVDNEppdyKSLI 392
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE----ARLR 815
                          490       500
                   ....*....|....*....|...
gi 544346093   393 PLERAVINGQL---YEESENQDE 412
Cdd:TIGR02169  816 EIEQKLNRLTLekeYLEKEIQEL 838
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
200-351 2.01e-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: 45.06  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   200 KIKELSQEVERL---KLKLKDMKAIEDDLMKTEdEYETLERRYANERDKAQfLSKELEHVKMELAKY--KLAEKTETSHE 274
Cdd:TIGR02169  192 IIDEKRQQLERLrreREKAERYQALLKEKREYE-GYELLKEKEALERQKEA-IERQLASLEEELEKLteEISELEKRLEE 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   275 qwLFKRLQEEEAKSGHL-SREVDALKEKIHEYMA----TEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKELER 349
Cdd:TIGR02169  270 --IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAeiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347

                   ..
gi 544346093   350 YR 351
Cdd:TIGR02169  348 ER 349
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
4-264 2.56e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    4 EKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTM 83
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   84 SEKLKKTEDKLQaassQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:TIGR04523 474 SRSINKIKQNLE----QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  164 LKNRLQSlEAIEKDFLKN-----KLNQDSGKSTTALHQENNKIKELSQEVERL--KLKLKDMKA--IEDDLMKTEDEYET 234
Cdd:TIGR04523 550 DDFELKK-ENLEKEIDEKnkeieELKQTQKSLKKKQEEKQELIDQKEKEKKDLikEIEEKEKKIssLEKELEKAKKENEK 628
                         250       260       270
                  ....*....|....*....|....*....|
gi 544346093  235 LERRYANERDKAQFLSKELEHVKMELAKYK 264
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2-177 2.84e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKL------------ 69
Cdd:COG4942   42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpp 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  70 --------------KTLTVM--FVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKM 133
Cdd:COG4942  122 lalllspedfldavRRLQYLkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 544346093 134 ysvtkerDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKD 177
Cdd:COG4942  202 -------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
15-361 3.07e-04

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: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.73  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   15 QECYSLKCNLEKERMTTKQLSQELESlkvRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKlKKTEDKL 94
Cdd:pfam07888  48 QAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE-KDALLAQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   95 QAASSQLQVE---------QNKVTTVTE--KLIEETKRALKSKTDVEEkmysvtkERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:pfam07888 124 RAAHEARIREleediktltQRVLERETEleRMKERAKKAGAQRKEEEA-------ERKQLQAKLQQTEEELRSLSKEFQE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  164 LKNRLQSLEAiEKDFLKNKLNQDSGKSTTAlhqennkikelSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYAN-- 241
Cdd:pfam07888 197 LRNSLAQRDT-QVLQLQDTITTLTQKLTTA-----------HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSma 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  242 -ERDKAQflsKELEHVKMELAKY--KLAEKTETSHE---QWlfkrLQEEEAksghLSREVDALKEKIheymatEDLICHL 315
Cdd:pfam07888 265 aQRDRTQ---AELHQARLQAAQLtlQLADASLALREgraRW----AQERET----LQQSAEADKDRI------EKLSAEL 327
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 544346093  316 QGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 361
Cdd:pfam07888 328 QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
46 PHA02562
endonuclease subunit; Provisional
62-300 3.40e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  62 LKEDLTKLKTLTVMfvderktmsEKLKKteDKLQAASSQLQVEQNKVTTVTEKL------IEETKRalKSKTDVEEKMYS 135
Cdd:PHA02562 155 LVEDLLDISVLSEM---------DKLNK--DKIRELNQQIQTLDMKIDHIQQQIktynknIEEQRK--KNGENIARKQNK 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 136 VTKERDDLKNkLKAEEEKGNDLLSRVNM------------------LKNRLQSLEAIEKDFLKNklnQDSGKSTTALHQE 197
Cdd:PHA02562 222 YDELVEEAKT-IKAEIEELTDELLNLVMdiedpsaalnklntaaakIKSKIEQFQKVIKMYEKG---GVCPTCTQQISEG 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 198 NNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEY--------------ETLERRYANERDKAQFLSKELEHVKMELAKY 263
Cdd:PHA02562 298 PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqskkllelknkiSTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 544346093 264 KLAEKTETSHEQWLFKRLQEEEAKSGHLSREVDALKE 300
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
83-247 3.94e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  83 MSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKlIEETKRALKS-KTDVEEKMYSVTKERDDLKNKLKAEEEKGN------ 155
Cdd:COG3883   28 LQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKlQAEIAEAEAEIEERREELGERARALYRSGGsvsyld 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 156 ---------DLLSRVNMLK----NRLQSLEAIEKDflKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIE 222
Cdd:COG3883  107 vllgsesfsDFLDRLSALSkiadADADLLEELKAD--KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
                        170       180
                 ....*....|....*....|....*
gi 544346093 223 DDLMKTEDEYETLERRYANERDKAQ 247
Cdd:COG3883  185 AQLSAEEAAAEAQLAELEAELAAAE 209
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
34-377 5.37e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.14  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   34 LSQELESLKVRIKELEAIESRLEKTEFTLK------EDLTKLKTlTVMFVDERKTM--------SEKLKKTedklQAASS 99
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSDKVKKLEATVEtykkklEDLGDLRR-QVKLLEERNAEymqrtlqlEEELKKA----NALRG 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  100 QLQVEQNKVTTVTEKLIEETKRALKSKTD---VEEKMYSVTK-------ERDDLK---NKLKAEEEKGNDLLSRVNMLKN 166
Cdd:pfam05622 184 QLETYKRQVQELHGKLSEESKKADKLEFEykkLEEKLEALQKekerliiERDTLRetnEELRCAQLQQAELSQADALLSP 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  167 RLQSLEAIEKDFLKNKLnqdsgKSTTALHQENNKIKELSQEvERLKLKLKDMKAIEDDLMKTEDEYETlERRYANERdka 246
Cdd:pfam05622 264 SSDPGDNLAAEIMPAEI-----REKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNELET-QNRLANQR--- 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  247 qflSKELEHvkmelakyklaektetsHEQWLFKRLQEEEAK---SGHLSREVDALKEKIHEYmatedlichlqgdHSVLQ 323
Cdd:pfam05622 334 ---ILELQQ-----------------QVEELQKALQEQGSKaedSSLLKQKLEEHLEKLHEA-------------QSELQ 380
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093  324 KKLNQQENR----NRDLGREIENLTKEL-----------ERYRHFS-------KSLRPSLNGRRISDPQVFSKEVQ 377
Cdd:pfam05622 381 KKKEQIEELepkqDSNLAQKIDELQEALrkkdedmkameERYKKYVekaksviKTLDPKQNPASPPEIQALKNQLL 456
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
23-373 5.78e-04

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: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   23 NLEKERmttkqLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTV---MFVD---ERKTMSEKLKKTEDkLQA 96
Cdd:pfam05557 131 NSELEE-----LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFeiqSQEQdseIVKNSKSELARIPE-LEK 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   97 ASSQLQVEQNKVTTVTEK--LIEETKRALKSKTDVEEKMYS------VTKER----------------------DDLKNK 146
Cdd:pfam05557 205 ELERLREHNKHLNENIENklLLKEEVEDLKRKLEREEKYREeaatleLEKEKleqelqswvklaqdtglnlrspEDLSRR 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  147 LKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKSTtalhQENNKIKELSQEVERLKLKL------KD-MK 219
Cdd:pfam05557 285 IEQLQQREIVLKEENSSLTSSARQLEKARRE-LEQELAQYLKKIE----DLNKKLKRHKALVRRLQRRVllltkeRDgYR 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  220 AI----EDDLMKTEDEYETLERRYANER--DKAQFLSKELEH----VKMELAKYKLAEKTETSHEQWLfkRLQEEEAKSG 289
Cdd:pfam05557 360 AIlesyDKELTMSNYSPQLLERIEEAEDmtQKMQAHNEEMEAqlsvAEEELGGYKQQAQTLERELQAL--RQQESLADPS 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  290 HLSREVDALKEKIHEYMAT-----------EDLICH--LQGD-----HSVLQKKLNQQENRNRDLGREIENLTKELERYR 351
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELErqrlreqknelEMELERrcLQGDydpkkTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLK 517
                         410       420
                  ....*....|....*....|..
gi 544346093  352 HFSKSLRPSLNGRRISDPQVFS 373
Cdd:pfam05557 518 RLLKKLEDDLEQVLRLPETTST 539
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-217 6.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   23 NLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQ 102
Cdd:COG4913   672 ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE-------KELEQAEEELDELQDRLEAAEDLAR 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  103 VEQnkvttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN------------------ML 164
Cdd:COG4913   745 LEL-------RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetadldadleslpEY 817
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093  165 KNRLQSLEAI-----EKDFlKNKLNQDSGKSTTALHQE-NNKIKELSQEVERLKLKLKD 217
Cdd:COG4913   818 LALLDRLEEDglpeyEERF-KELLNENSIEFVADLLSKlRRAIREIKERIDPLNDSLKR 875
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
25-236 6.57e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 6.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  25 EKERMTTKQLSQELESLKVRIKELEAIESRLEKTEfTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAAS---SQL 101
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLR-------EKREALAELNDERRERLAEKRerkREL 639
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 102 --QVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLknklkaeeekgndlLSRVNMLKNRLQSLEAI--EKD 177
Cdd:PRK02224 640 eaEFDEARI----EEAREDKERAEEYLEQVEEKLDELREERDDL--------------QAEIGAVENELEELEELreRRE 701
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093 178 FLKNKLnqdsgKSTTALHQENNKIKEL---------SQEVERLKLKLKDMKaiedDLMKTEDEYETLE 236
Cdd:PRK02224 702 ALENRV-----EALEALYDEAEELESMygdlraelrQRNVETLERMLNETF----DLVYQNDAYSHIE 760
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
36-239 6.80e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  36 QELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvdERKTMSEKLKKTEDKLQAAssqlqveqnkvttvtEKL 115
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKT-------ELEDLEKEIKRLELEIEEV---------------EAR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 116 IEETKRALKSKTDVEEkMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDfLKNKLNQDSGKSTTALH 195
Cdd:COG1579   75 IKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 544346093 196 QENNKIKELSQEVERLKlklkdmKAIEDDLMKtedEYETLERRY 239
Cdd:COG1579  153 ELEAELEELEAEREELA------AKIPPELLA---LYERIRKRK 187
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
84-302 7.21e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  84 SEKLKKTEDKLQAASSQLQVEQNKVttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNM 163
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 164 LKNRLQSLEAIEKDFLKN-KLNQDSGKSTTALHQEN-----NKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLER 237
Cdd:COG4942   95 LRAELEAQKEELAELLRAlYRLGRQPPLALLLSPEDfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544346093 238 RYANERDKAQFLSKELEHVKMELAKY-KLAEKTETSHEQwlfkRLQEEEAKSGHLSREVDALKEKI 302
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLlARLEKELAELAA----ELAELQQEAEELEALIARLEAEA 236
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2-395 7.49e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 7.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093     2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQL---SQELESLKVRIKELEAIESRLEK---TEFTLKEDLTKLKTLTvm 75
Cdd:TIGR00618  301 AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHvkqQSSIEEQRRLLQTLHSQEIHIRDaheVATSIREISCQQHTLT-- 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    76 fvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEEtkRALKSKTDVEEKMYSVTKERDDLK--------NKL 147
Cdd:TIGR00618  379 --QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQLAHAKKQQELQQRYAELCaaaitctaQCE 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   148 KAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKD-----MKAIE 222
Cdd:TIGR00618  455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrMQRGE 534
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   223 DDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAK-------YKLAEKTETSHEQWLFKRLQEEEAKSGHLSREV 295
Cdd:TIGR00618  535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqcdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   296 DALKEKIHEYMATEDLICHLQGDHSVLQKKLNQqenrnrdLGREIENLTKELERYRHFSKSLRPSLNG-RRISDPQVFSK 374
Cdd:TIGR00618  615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-------LHALQLTLTQERVREHALSIRVLPKELLaSRQLALQKMQS 687
                          410       420
                   ....*....|....*....|.
gi 544346093   375 EVQTEAVDNEPPDYKSLIPLE 395
Cdd:TIGR00618  688 EKEQLTYWKEMLAQCQTLLRE 708
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
51-299 8.13e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  51 IESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIE---ETKRALKSKT 127
Cdd:COG4372    4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 128 DVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDF--LKNKLNQDSGKSTTALHQENNKIKELS 205
Cdd:COG4372   84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLeaQIAELQSEIAEREEELKELEEQLESLQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 206 QEVERLKLKLKDMKAIE-----DDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYKLAEKTETSHEQWLFKR 280
Cdd:COG4372  164 EELAALEQELQALSEAEaeqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
                        250
                 ....*....|....*....
gi 544346093 281 LQEEEAKSGHLSREVDALK 299
Cdd:COG4372  244 LEEDKEELLEEVILKEIEE 262
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
3-233 9.12e-04

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: 41.55  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    3 LEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELeaiESRLEKTEFTLKEDLTKLKTLTVMfVDE--- 79
Cdd:pfam00261   3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLL---EEELERTEERLAEALEKLEEAEKA-ADEser 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   80 -RKTMSEKLKKTEDKLQAASSQLqveqnkvttvtEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLL 158
Cdd:pfam00261  79 gRKVLENRALKDEEKMEILEAQL-----------KEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELE 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093  159 SRVNMLKNRLQSLEAIEKdflknKLNQDSGKSTTALHQENNKIKEL---SQEVERLKLKL-KDMKAIEDDLMKTEDEYE 233
Cdd:pfam00261 148 EELKVVGNNLKSLEASEE-----KASEREDKYEEQIRFLTEKLKEAetrAEFAERSVQKLeKEVDRLEDELEAEKEKYK 221
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2-211 1.00e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTltvmfvdERK 81
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  82 TMSEKLKKTEDKL--QAASSQLQVEQNKVTTV--------TEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEE 151
Cdd:COG4942   94 ELRAELEAQKEELaeLLRALYRLGRQPPLALLlspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 152 EKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERL 211
Cdd:COG4942  174 AELEALLAELEEERAALEALKA-ERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
36-370 1.11e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  36 QELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDE---------------------RKTMSEKLKKTEDKL 94
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglddadaeavearREELEDRDEELRDRL 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  95 QAASSQLQVEQNKVTTVTEKL--------------------IEETKRALKSK----TDVEEKMYSVTKERDDLKNKLKAE 150
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDAddleeraeelreeaaeleseLEEAREAVEDRreeiEELEEEIEELRERFGDAPVDLGNA 410
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 151 EEKGNDLLSRVNMLKNRLQSLEA----IEKDFLKNKLNQDSGKSTT------------ALHQENNKIKELSQEVERLKLK 214
Cdd:PRK02224 411 EDFLEELREERDELREREAELEAtlrtARERVEEAEALLEAGKCPEcgqpvegsphveTIEEDRERVEELEAELEDLEEE 490
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 215 ----------LKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMElaKYKLAEKTETSHEQWLFKRLQEE 284
Cdd:PRK02224 491 veeveerlerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER--AAELEAEAEEKREAAAEAEEEAE 568
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 285 EAKS--GHLSREVDALKEKIHEYMATEDL---ICHLQGDHSVLQKKLNQQENRNrDLGReiENLTKELERYRhfskSLRP 359
Cdd:PRK02224 569 EAREevAELNSKLAELKERIESLERIRTLlaaIADAEDEIERLREKREALAELN-DERR--ERLAEKRERKR----ELEA 641
                        410
                 ....*....|.
gi 544346093 360 SLNGRRISDPQ 370
Cdd:PRK02224 642 EFDEARIEEAR 652
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
32-348 1.34e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   32 KQLSQELESLKVRIK----ELEAIESRLEKTEFTLKEDLTKLKTLTvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNK 107
Cdd:TIGR04523  36 KQLEKKLKTIKNELKnkekELKNLDKNLNKDEEKINNSNNKIKILE----QQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  108 VTTVTE---KLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDllsrvnmLKNRLQSLEAIEKDFLKNKLN 184
Cdd:TIGR04523 112 IKNDKEqknKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELNLLEKEKLN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  185 QdsgksttalhqeNNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKYK 264
Cdd:TIGR04523 185 I------------QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  265 LAEKTETSHEQWLFKRLQEEEaksghlsREVDALKEKIHEymaTEDLICHLQGDHSVLQKKlnQQENRNRDLGREIENLT 344
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQ-------KELEQNNKKIKE---LEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQE 320

                  ....
gi 544346093  345 KELE 348
Cdd:TIGR04523 321 KKLE 324
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
147-352 1.43e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  147 LKAEEEKgnDLLSRVNMLKNRLQSL--EAIEKDFLKNKLNQDsgKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDD 224
Cdd:COG4913   245 EDAREQI--ELLEPIRELAERYAAAreRLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  225 LmktEDEYETLERRYA-NERDKAQFLSKELEHVKMELAKyklAEKTETSHEQWLfKRLQEEEAKSghlSREVDALKEKIH 303
Cdd:COG4913   321 L---REELDELEAQIRgNGGDRLEQLEREIERLERELEE---RERRRARLEALL-AALGLPLPAS---AEEFAALRAEAA 390
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 544346093  304 EYMATedlichLQGDHSVLQKKLNQQENRNRDLGREIENLTKELERYRH 352
Cdd:COG4913   391 ALLEA------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-233 1.54e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  21 KCNLEKERMTTKQLSQEL-ESLKVRIKELEAIESRLEKteftLKEDLTKLKTltvmfvdERKTMSEKLKKTEDKLQAASS 99
Cdd:COG4372   12 RLSLFGLRPKTGILIAALsEQLRKALFELDKLQEELEQ----LREELEQARE-------ELEQLEEELEQARSELEQLEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 100 QLQVEQNKVTTVTEKLI---EETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEK 176
Cdd:COG4372   81 ELEELNEQLQAAQAELAqaqEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544346093 177 DFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYE 233
Cdd:COG4372  161 SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2-133 1.67e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   2 ALEKLEDAFNKSKQECYSLKCNLEKERMTTKQLSQELESLKVRI-------------KELEAIESRLEktefTLKEDLTK 68
Cdd:COG1579   32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkyeeqlgnvrnnKEYEALQKEIE----SLKRRISD 107
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346093  69 LKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKM 133
Cdd:COG1579  108 LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
46-346 2.08e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.74  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   46 KELEAIESRLEKTEFT-----LKEDLTKLKTLTVMFVDERKTMSEKLKKTED-------KLQAASSQLQVEQNKVTTVT- 112
Cdd:PTZ00440  940 KEKEKIEKQLSDTKINnlkmqIEKTLEYYDKSKENINGNDGTHLEKLDKEKDewehfksEIDKLNVNYNILNKKIDDLIk 1019
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  113 ---EKLIEETKRALKSK-TDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIEKDFLKNklnqdsg 188
Cdd:PTZ00440 1020 kqhDDIIELIDKLIKEKgKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKK------- 1092
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  189 ksttalhqennkIKELSQEVERLKLKLKDMKAIEDDLM-KTEDEYET----LERRYANERDkaqfLSKELEHVKMELAKY 263
Cdd:PTZ00440 1093 ------------IDENKNKLIEIKNKSHEHVVNADKEKnKQTEHYNKkkksLEKIYKQMEK----TLKELENMNLEDITL 1156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  264 KLAEKTETSHEQWLF----KRLQEEEAKSGHLSREVDALKEKIHEYMAteDLICHLQGDHSVLqkKLNQQENRNRDLGRE 339
Cdd:PTZ00440 1157 NEVNEIEIEYERILIdhivEQINNEAKKSKTIMEEIESYKKDIDQVKK--NMSKERNDHLTTF--EYNAYYDKATASYEN 1232

                  ....*..
gi 544346093  340 IENLTKE 346
Cdd:PTZ00440 1233 IEELTTE 1239
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-243 2.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  22 CNLEKERMTTKQLSQELESLKVRIKELEAIESRLE---KTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEdKLQAAS 98
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlvEAEDRIERLEERREDLEELIAERRETIEEKRERAE-ELRERA 546
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  99 SQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLkNKLKAEEEKGNDLLSRVNMLKNRLQSLEAIE--- 175
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNder 625
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 176 KDFLKNK------------------LNQDSGKSTTALHQENNKIKELS-----------------QEVERLKLKLKDMKA 220
Cdd:PRK02224 626 RERLAEKrerkreleaefdearieeAREDKERAEEYLEQVEEKLDELReerddlqaeigavenelEELEELRERREALEN 705
                        250       260
                 ....*....|....*....|...
gi 544346093 221 IEDDLMKTEDEYETLERRYANER 243
Cdd:PRK02224 706 RVEALEALYDEAEELESMYGDLR 728
46 PHA02562
endonuclease subunit; Provisional
8-250 2.27e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   8 DAFNKSK--------QECYSLKCNLEKERMTTKQLSQELESL-KVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVD 78
Cdd:PHA02562 169 DKLNKDKirelnqqiQTLDMKIDHIQQQIKTYNKNIEEQRKKnGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  79 ERKTMSEKLKKTEDKLQAASSQLQ--------VEQNKVT-TVTEKLIEETKRAlkskTDVEEKMYSVTKERDDLKNKLKA 149
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEqfqkvikmYEKGGVCpTCTQQISEGPDRI----TKIKDKLKELQHSLEKLDTAIDE 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 150 EEEKGNDLlsrvNMLKNRLQSleaiekdfLKNKLNQDSGksttALHQENNKIKELSQEVERLKLKLKDmkaIEDDLMKTE 229
Cdd:PHA02562 325 LEEIMDEF----NEQSKKLLE--------LKNKISTNKQ----SLITLVDKAKKVKAAIEELQAEFVD---NAEELAKLQ 385
                        250       260
                 ....*....|....*....|....
gi 544346093 230 DEYETLERRYAN---ERDKAQFLS 250
Cdd:PHA02562 386 DELDKIVKTKSElvkEKYHRGIVT 409
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
138-302 2.29e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 138 KERDDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEAiEKDFLKNKLNQDSGKSTTAlhqENNK-IKELSQEVERLKLKLK 216
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-EIEEVEARIKKYEEQLGNV---RNNKeYEALQKEIESLKRRIS 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 217 DmkaIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVKMELAKyKLAEktetsheqwlfkrLQEEEAKsghLSREVD 296
Cdd:COG1579  107 D---LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE-ELAE-------------LEAELEE---LEAERE 166

                 ....*.
gi 544346093 297 ALKEKI 302
Cdd:COG1579  167 ELAAKI 172
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
86-310 3.49e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  86 KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKmysvTKERDDLKNKLKAEEEKgndLLSRVNMLK 165
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAE---IEERREELG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 166 NRLQSLeaiekdflknklnQDSGKSTTALHQ--ENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANER 243
Cdd:COG3883   90 ERARAL-------------YRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544346093 244 DKAQFLSKELEHVKMELAKyKLAEKTETSHEqwLFKRLQEEEAKSGHLSREVDALKEKIHEYMATED 310
Cdd:COG3883  157 AELEALKAELEAAKAELEA-QQAEQEALLAQ--LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
32-122 3.54e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  32 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLtvmfVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTV 111
Cdd:COG4942  153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
                         90
                 ....*....|.
gi 544346093 112 TEKLIEETKRA 122
Cdd:COG4942  229 IARLEAEAAAA 239
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
22-81 3.84e-03

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 39.12  E-value: 3.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   22 CNLEKERmttKQLSQELESLKVRIKELEAiesRLEKTEFTLKEDLTKLKTLTVMFVDERK 81
Cdd:pfam09727 133 YLLEKER---ERLKQELEQEKAQQKRLEK---ELKKLLEKLEEELSKQKQIALLLVKERK 186
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
86-349 3.91e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   86 KLKKTEDKLQAASSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEkmysVTKERDDLKNKLKAEEEKGNDLLSRVNMLK 165
Cdd:TIGR04523  34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKI----LEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  166 NRLQSleaieKDFLKNKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLERRYANERDK 245
Cdd:TIGR04523 110 SEIKN-----DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  246 AQflsKELEHVKMELAK--YKLAE-KTETSHEQWLFKRLQEEEAKSGHLSREVDALKEKIHEymatedlichLQGDHSVL 322
Cdd:TIGR04523 185 IQ---KNIDKIKNKLLKleLLLSNlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE----------KTTEISNT 251
                         250       260
                  ....*....|....*....|....*..
gi 544346093  323 QKKLNQQENRNRDLGREIENLTKELER 349
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQ 278
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
31-460 4.03e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    31 TKQLSQELESLKVRIKELEAIESRLEKTeftLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTT 110
Cdd:TIGR00606  446 KEILEKKQEELKFVIKELQQLEGSSDRI---LELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   111 VTEKLIEETkralksktDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRV-------NMLKNRLQSLEA---IEKDFLK 180
Cdd:TIGR00606  523 EMEQLNHHT--------TTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKeinQTRDRLA 594
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   181 nKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDM---KAIEDDLMKTEDEYETLERRYANERDKAQFLSKELEHVK 257
Cdd:TIGR00606  595 -KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   258 ME------LAKYKLAEKTETsheQWLFKRLQEEEAKSGHLSREVDALKEKIHEymATEDLICHLQGDHSVLQ---KKLNQ 328
Cdd:TIGR00606  674 DEnqsccpVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEK--RRDEMLGLAPGRQSIIDlkeKEIPE 748
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   329 QENRNRDLGREIENLTKELERYRHFSKSLRPSLNGRRISDPQV-FSKEVQTEAVDNEpPDYKSLIPLERAVINGQLYEES 407
Cdd:TIGR00606  749 LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtIMERFQMELKDVE-RKIAQQAAKLQGSDLDRTVQQV 827
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 544346093   408 ENQDEDPNDEGSVLSFKCSQSTPCPVNRKLWIPWMKSKEGHLQNGKMQTKPNA 460
Cdd:TIGR00606  828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL 880
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
151-347 4.88e-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: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  151 EEKGNDLL---SRVNMLKNRLQSLEAIEKDFLK------NKLNQDSGKSTTALHQENNKIKELSQEVERLKLKLKDMKAI 221
Cdd:pfam07888  16 EEGGTDMLlvvPRAELLQNRLEECLQERAELLQaqeaanRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  222 EDDLMKTEDEYETLERRYANERD-------KAQFLSKELEHVKMELAKYKLAEKTEtsheqwlFKRLQEEEAKSGHLSRE 294
Cdd:pfam07888  96 HEELEEKYKELSASSEELSEEKDallaqraAHEARIRELEEDIKTLTQRVLERETE-------LERMKERAKKAGAQRKE 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 544346093  295 VDALKEKIHEYM-ATEDLICHLQGDHSVLQKKLNQQENRNRDLGREIENLTKEL 347
Cdd:pfam07888 169 EEAERKQLQAKLqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL 222
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
3-228 5.65e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    3 LEKLEDAFNKSKQecyslkcNLEKERMTTKQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKT 82
Cdd:TIGR04523 470 LKVLSRSINKIKQ-------NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   83 MSEKLKKTEDKLQaaSSQLQVEQNKVTTVTEKLIEETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKGNDLLSRVN 162
Cdd:TIGR04523 543 LEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544346093  163 MLKNRLQSLEAIEK--DFLKNKLNQdsgkSTTALHQENNKIKELSQEVERlklKLKDMKAIEDDLMKT 228
Cdd:TIGR04523 621 KAKKENEKLSSIIKniKSKKNKLKQ----EVKQIKETIKEIRNKWPEIIK---KIKESKTKIDDIIEL 681
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
24-361 5.86e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    24 LEKERMTTKQLSQELESLKVRIKELEAIESRLEK--------TEFTLKeDLTKLKTLTVMFVDERKTMS----EKLKKTE 91
Cdd:TIGR00606  257 IEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgTDEQLN-DLYHNHQRTVREKERELVDCqrelEKLNKER 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    92 DKLQAASSQLQVEQNKVTTVTEKLIEETKR--------ALKSKTDVEEKMYSVTKErddLKNKLKAEEEKGNDLLSRVNM 163
Cdd:TIGR00606  336 RLLNQEKTELLVEQGRLQLQADRHQEHIRArdsliqslATRLELDGFERGPFSERQ---IKNFHTLVIERQEDEAKTAAQ 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   164 LKNRLQSLEAIEKDFLKNKLNQDSGKSTT------ALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYETLER 237
Cdd:TIGR00606  413 LCADLQSKERLKQEQADEIRDEKKGLGRTielkkeILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK 492
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   238 RYANERDKAQFLSKELEHVKMELAKYKLAEKTE------TSHEQWLF---KRLQEEEAKSGHLSREVDALKEKIHEYMAT 308
Cdd:TIGR00606  493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNK 572
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 544346093   309 EDLICHLqgdHSvLQKKLNQQENRNRDLGREIENLTKELERYRHFSKSLRPSL 361
Cdd:TIGR00606  573 KQLEDWL---HS-KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
32-288 6.05e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    32 KQLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTV 111
Cdd:pfam01576   99 KKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSL 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   112 TEklieetkraLKSK-----TDVEEKMYSVTKERDDL-KNKLKAEEEKGN------DLLSRVNMLKNRLQSLEAiEKDFL 179
Cdd:pfam01576  179 SK---------LKNKheamiSDLEERLKKEEKGRQELeKAKRKLEGESTDlqeqiaELQAQIAELRAQLAKKEE-ELQAA 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   180 KNKLNQDSGKSTTALhqenNKIKELSQEVERLklklkdmkaiEDDLmktEDEYETLERRYANERDkaqfLSKELEHVKME 259
Cdd:pfam01576  249 LARLEEETAQKNNAL----KKIRELEAQISEL----------QEDL---ESERAARNKAEKQRRD----LGEELEALKTE 307
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 544346093   260 L--------AKYKLAEKTETshEQWLFKRLQEEEAKS 288
Cdd:pfam01576  308 LedtldttaAQQELRSKREQ--EVTELKKALEEETRS 342
GrpE pfam01025
GrpE;
189-247 6.17e-03

GrpE;


Pssm-ID: 425996 [Multi-domain]  Cd Length: 165  Bit Score: 37.97  E-value: 6.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 544346093  189 KSTTALHQENNKIKELSQEVERLKLKLKDMKaieDDLMKTEDEYETLERRYANERDKAQ 247
Cdd:pfam01025   1 EEKKNEEALTDEIESLEEEIEELEKKIEELK---EKLLRALAEFENLRKRTEKEKEEAK 56
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
33-273 6.22e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 39.67  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   33 QLSQELESLKVRIKELEAIESRLEKTEFTLKEDLTKLktltvmfvderktmSEKLKKTEDKLQAASSQLQVEQNKVTTvT 112
Cdd:pfam19220  38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGL--------------TRRLSAAEGELEELVARLAKLEAALRE-A 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  113 EKLIEETKRALKSKTDVEEkmysvtkerdDLKNKLKAEEEKGNDLLSRVNMLKNRLQSLEA--IEKDFLKNKLNQDSGKS 190
Cdd:pfam19220 103 EAAKEELRIELRDKTAQAE----------ALERQLAAETEQNRALEEENKALREEAQAAEKalQRAEGELATARERLALL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  191 TTALHQENNKIKELSQEVERLKLKLKDMKAIEDDLMKTEDEYET--LERRYANERDKAQFlskELEHVKMELAKYKLAEK 268
Cdd:pfam19220 173 EQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGqlAAEQAERERAEAQL---EEAVEAHRAERASLRMK 249

                  ....*
gi 544346093  269 TETSH 273
Cdd:pfam19220 250 LEALT 254
MPS2 pfam17060
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ...
156-303 7.19e-03

Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.


Pssm-ID: 407228 [Multi-domain]  Cd Length: 340  Bit Score: 39.19  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093  156 DLLSRVNMLKNRLQSleAIEKDFLKNKLNQDSGKSTTalhQENNKIKELSQEVERLKLKLKDMkaiEDDLMKTEDEYETL 235
Cdd:pfam17060 109 DVKSSPRSEADSLGT--PIKVDLLRNLKPQESPETPR---RINRKYKSLELRVESMKDELEFK---DETIMEKDRELTEL 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544346093  236 ERRYANERDKAQFLSKELEHVKME-LAKYKLAEKTETSHE---QWLFKRLQEEEAKSGHLSREVDALKEKIH 303
Cdd:pfam17060 181 TSTISKLKDKYDFLSREFEFYKQHhEHGGNNSIKTATKHEfiiSELKRKLQEQNRLIRILQEQIQFDPGALH 252
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
13-152 7.58e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 39.66  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   13 SKQECYSLKcnLEKERMTT--KQLSQELESLKVRIKELEaiesrleKTEFTLKEDLTKLKTLTVMFVDERKTMSEKLKKT 90
Cdd:pfam05911 686 LKEEFEQLK--SEKENLEVelASCTENLESTKSQLQESE-------QLIAELRSELASLKESNSLAETQLKCMAESYEDL 756
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346093   91 EDKLQAASSQLQVEQNKVTTVTEKLIEETK---RALKSKTDVEEKMYSVTKER------DDLKNKLKAEEE 152
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEALEVELEEEKNcheELEAKCLELQEQLERNEKKEssncdaDQEDKKLQQEKE 827
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
37-214 8.76e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093    37 ELESLKV----RIKELEAIESRLEKTEFTLKEDLTKLKtltvmfvDERKTMSEKLKKTEDKLQAASSQLQVEQNKVTTVT 112
Cdd:smart00787 127 RLEAKKMwyewRMKLLEGLKEGLDENLEGLKEDYKLLM-------KELELLNSIKPKLRDRKDALEEELRQLKQLEDELE 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093   113 EKLIEETKRA-LKSKTDVEEKMYSVtKERDDLKNKLKAEEEKGNDLlsrVNMLKNRLQSLEAIEKDFLKNKlnqdsgkst 191
Cdd:smart00787 200 DCDPTELDRAkEKLKKLLQEIMIKV-KKLEELEEELQELESKIEDL---TNKKSELNTEIAEAEKKLEQCR--------- 266
                          170       180
                   ....*....|....*....|...
gi 544346093   192 talHQENNKIKELSQEVERLKLK 214
Cdd:smart00787 267 ---GFTFKEIEKLKEQLKLLQSL 286
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
117-199 9.52e-03

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 39.42  E-value: 9.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346093 117 EETKRALKSKTDVEEKMYSVTKERDDLKNKLKAEEEKgnDLLSRVNMLKNRLQS--LEAIeKDFLKnKLNQDSGKSTTAL 194
Cdd:PTZ00400 561 EKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKD--ELKQKITKLRSTLSSedVDSI-KDKTK-QLQEASWKISQQA 636

                 ....*
gi 544346093 195 HQENN 199
Cdd:PTZ00400 637 YKQGN 641
 
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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