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Conserved domains on  [gi|2564278|emb|CAA75400|]
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leucine zipper protein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 7-481 6.42e-29

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 120.94  E-value: 6.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278       7 EPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNPRF 83
Cdd:TIGR02169  534 GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDPKY 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278      84 DKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNE- 162
Cdd:TIGR02169  613 EPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREl 690

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     163 -NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:TIGR02169  691 sSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     242 KAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRETE 318
Cdd:TIGR02169  771 EEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLK 846

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     319 GGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLK 398
Cdd:TIGR02169  847 EQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     399 KKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELDRGYKS 477
Cdd:TIGR02169  925 KLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004


                   ....
gi 2564278     478 IMEL 481
Cdd:TIGR02169 1005 ILER 1008
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-481 6.42e-29

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: 120.94  E-value: 6.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278       7 EPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNPRF 83
Cdd:TIGR02169  534 GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDPKY 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278      84 DKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNE- 162
Cdd:TIGR02169  613 EPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREl 690

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     163 -NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:TIGR02169  691 sSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     242 KAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRETE 318
Cdd:TIGR02169  771 EEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLK 846

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     319 GGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLK 398
Cdd:TIGR02169  847 EQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     399 KKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELDRGYKS 477
Cdd:TIGR02169  925 KLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004


                   ....
gi 2564278     478 IMEL 481
Cdd:TIGR02169 1005 ILER 1008
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 4-106 1.03e-25

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 101.54  E-value: 1.03e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278       4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYPETNDAIPMIS 75
Cdd:smart00968  11 ISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLPEPGFVGPAID 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2564278      76 KLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 106
Cdd:smart00968  90 LVEYDPELRPALEYLLGNTLVVDDLETARRL 120
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 4-107 9.91e-22

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 90.01  E-value: 9.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278      4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAIPMISKLRYNP 81
Cdd:pfam06470  12 IEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAGPLLDLVEYDD 90

                          90       100
                  ....*....|....*....|....*.
gi 2564278     82 RFDKAFKHVFGKTLICRSMEVSTQLA 107
Cdd:pfam06470  91 EYRKALRYLLGNTLVVDDLDEALELA 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-473 2.03e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  165 RRNIERINNEIDQLMNQMQQIETQQRK------FKASRDSILSEMKMLKEKRQQSEktfmpkqrsLQSLEASLHAMESTR 238
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAE---------LEELEAELEELEAEL 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  239 ESLKAELgtDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETyLNENLRKRLDQVEQELNELRETE 318
Cdd:COG1196 256 EELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEEL 332

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  319 GG--TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 396
Cdd:COG1196 333 EEleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2564278  397 LKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELDR 473
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-483 1.73e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   163 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 239
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   240 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 319
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   320 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 394
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   395 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 460
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474

                        330       340
                 ....*....|....*....|...
gi 2564278   461 KERLIKRQEELDRGYKSIMELMK 483
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIK 497
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-481 6.42e-29

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: 120.94  E-value: 6.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278       7 EPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDV--RDTAYPETNDAIPM-ISKLRYNPRF 83
Cdd:TIGR02169  534 GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKA-GRATFLPLNKMRDerRDLSILSEDGVIGFaVDLVEFDPKY 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278      84 DKAFKHVFGKTLICRSMEVSTQLARAFTMdcITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNE- 162
Cdd:TIGR02169  613 EPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREl 690

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     163 -NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:TIGR02169  691 sSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     242 KAELGTdllSQLSLEDQKRVDAlNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRL---DQVEQELNELRETE 318
Cdd:TIGR02169  771 EEDLHK---LEEALNDLEARLS-HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEyleKEIQELQEQRIDLK 846

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     319 GGTVltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLK 398
Cdd:TIGR02169  847 EQIK--SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     399 KKEECMKKIRELGSLPQEAFE-KYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELDRGYKS 477
Cdd:TIGR02169  925 KLEALEEELSEIEDPKGEDEEiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004


                   ....
gi 2564278     478 IMEL 481
Cdd:TIGR02169 1005 ILER 1008
SMC_hinge smart00968
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ...
 4-106 1.03e-25

SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 214944 [Multi-domain]  Cd Length: 120  Bit Score: 101.54  E-value: 1.03e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278       4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLD--------VRDTAYPETNDAIPMIS 75
Cdd:smart00968  11 ISVDPKYETALEAALGGRLQAVVVDTEETAKKAI-EFLKKNRLGRATFLPLDKIKprspagskLREALLPEPGFVGPAID 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2564278      76 KLRYNPRFDKAFKHVFGKTLICRSMEVSTQL 106
Cdd:smart00968  90 LVEYDPELRPALEYLLGNTLVVDDLETARRL 120
SMC_hinge pfam06470
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ...
 4-107 9.91e-22

SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.


Pssm-ID: 461926 [Multi-domain]  Cd Length: 116  Bit Score: 90.01  E-value: 9.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278      4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLpGEVTFLPLNKLDVRDTAYPET--NDAIPMISKLRYNP 81
Cdd:pfam06470  12 IEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKL-GRATFLPLDRLKPRPRRPGADlkGGAGPLLDLVEYDD 90

                          90       100
                  ....*....|....*....|....*.
gi 2564278     82 RFDKAFKHVFGKTLICRSMEVSTQLA 107
Cdd:pfam06470  91 EYRKALRYLLGNTLVVDDLDEALELA 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-482 4.45e-20

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: 93.97  E-value: 4.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278       4 FECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLR----- 78
Cdd:TIGR02168  529 ISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakdl 607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278      79 --YNPRFDKAFKHVFGKTLICRSMEVSTQLARA--FTMDCITLEGDQVSHRGALTGGYYDTRKSRL-------ELQKDVR 147
Cdd:TIGR02168  608 vkFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNSSILerrreieELEEKIE 687

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     148 KAEEELGELEAKLNEnLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTF-------MPK 220
Cdd:TIGR02168  688 ELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELteleaeiEEL 766

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     221 QRSLQSLEASLHAMESTRESLKAELgTDLLSQLSLEDqKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENL 300
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAATERRL-EDL 843

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     301 RKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKsmerwKNMEKEHmdA 378
Cdd:TIGR02168  844 EEQIEELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-----KRSELRR--E 916

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     379 INHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQE---AFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFV 455
Cdd:TIGR02168  917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996

                          490       500
                   ....*....|....*....|....*..
gi 2564278     456 NFSEQKERLIKRQEELDRGYKSIMELM 482
Cdd:TIGR02168  997 ELKERYDFLTAQKEDLTEAKETLEEAI 1023
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-473 2.03e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  165 RRNIERINNEIDQLMNQMQQIETQQRK------FKASRDSILSEMKMLKEKRQQSEktfmpkqrsLQSLEASLHAMESTR 238
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAE---------LEELEAELEELEAEL 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  239 ESLKAELgtDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETyLNENLRKRLDQVEQELNELRETE 318
Cdd:COG1196 256 EELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEEL 332

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  319 GG--TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 396
Cdd:COG1196 333 EEleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2564278  397 LKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELDR 473
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 168-367 1.75e-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: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     168 IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGT 247
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     248 dlLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELRETeggtvLTATT 327
Cdd:TIGR02169  383 --TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI-AGIEAKINELEEEKEDKALE-----IKKQE 454

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2564278     328 SELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMER 367
Cdd:TIGR02169  455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 137-366 1.85e-07

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: 53.91  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     137 KSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKT 216
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     217 FMPKQRSLQSLEASLHAMESTRESLKAELG--TDLLSQLSLEDQKrvdalndeIRQLQQENRQLLNE--RIKLEGIITRV 292
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEelREKLAQLELRLEG--------LEVRIDNLQERLSEeySLTLEEAEALE 960

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564278     293 ETYLN--ENLRKRLDQVEQELNELretegGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSME 366
Cdd:TIGR02168  961 NKIEDdeEEARRRLKRLENKIKEL-----GPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-424 2.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  242 KAELGTDLLSQLSLE-----DQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRE 316
Cdd:COG1196 315 EERLEELEEELAELEeeleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  317 TEggtvltATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGML 396
Cdd:COG1196 395 AA------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                       250       260
                ....*....|....*....|....*...
gi 2564278  397 LKKKEECMKKIRELGSLPQEAFEKYQTL 424
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLL 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 206-473 4.18e-07

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: 52.75  E-value: 4.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     206 LKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLK--AELGTDL------LSQLSLEDQ-KRVDALNDEIRQLQQENR 276
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLErqAEKAERYkelkaeLRELELALLvLRLEELREELEELQEELK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     277 QLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEA 356
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKE-----LYALANEISRLEQQKQILRERLANLERQLEELEA 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     357 GIKELQKSmerwknmekehmdaINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKyqtlsLKQLFRKLEQC 436
Cdd:TIGR02168  324 QLEELESK--------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR-----LEELEEQLETL 384

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2564278     437 NTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELDR 473
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-484 4.26e-07

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: 52.75  E-value: 4.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     162 ENLRRNIERINNEIDQLMNQMQQIETQQRK-----------FKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEAS 230
Cdd:TIGR02168  182 ERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelRELELALLVLRLEELREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     231 LHAMESTRESLKAELGTdlLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKR------L 304
Cdd:TIGR02168  262 LQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLdelaeeL 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     305 DQVEQELNELRE----------------TEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERW 368
Cdd:TIGR02168  340 AELEEKLEELKEelesleaeleeleaelEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     369 K-NMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLsLKQLFRKLEQCNTELkkysHVN 447
Cdd:TIGR02168  420 QqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA-LDAAERELAQLQARL----DSL 494

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2564278     448 KKALDQFVNFSEQKERLIKRQEELDRGYKSIMELMKC 484
Cdd:TIGR02168  495 ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 136-367 5.46e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 5.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  136 RKSRLELQKDVRKAEEELGELEAKLNENLRRnIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEK 215
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  216 TFMPKQRSLQSLEASLHAMESTRESLKAELgtdllsqlsLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETY 295
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEEL---------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2564278  296 LNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMER 367
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-472 9.15e-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: 51.61  E-value: 9.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     162 ENLRRNIERINNEIDQLMNQMQQIETQqrKFKASRDSILSEMKmlkEKRQQSEKTfmpkqRSLQSLEASLHAMESTRESL 241
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEK---REYEGYELL-----KEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     242 KAELGtdllsqlslEDQKRVDALNDEIRQLQQENRQLlNERIKLEGIITRVEtylnenLRKRLDQVEQELNELRETeggt 321
Cdd:TIGR02169  250 EEELE---------KLTEEISELEKRLEEIEQLLEEL-NKKIKDLGEEEQLR------VKEKIGELEAEIASLERS---- 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     322 vltattseLEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKnmekehmdainhdtKELEKMTNRqgmLLKKKE 401
Cdd:TIGR02169  310 --------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER--------------KRRDKLTEE---YAELKE 364

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564278     402 ECMKKIRELGSLPQEAFEKYQTLS-----LKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELD 472
Cdd:TIGR02169  365 ELEDLRAELEEVDKEFAETRDELKdyrekLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-483 1.73e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   163 NLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEktfmpkqRSLQSLEASLHAMESTRE--- 239
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEeie 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   240 SLKAELGTDLLSQLSLEDQKRvdALNDEIRQLQQENRQLLNERIKLEGIITRVETYlnENLRKRLDQVEQELNELRETEG 319
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIR--ELEERIEELKKEIEELEEKVKELKELKEKAEEY--IKLSEFYEEYLDELREIEKRLS 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   320 G-----TVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRqg 394
Cdd:PRK03918 318 RleeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE-- 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   395 mLLKKKEECMKKIREL----GSLPQEAFEKYQTLS-LKQLFRKLEQCNTEL---------KKYSHVNKKALDQFVNFSEQ 460
Cdd:PRK03918 396 -LEKAKEEIEEEISKItariGELKKEIKELKKAIEeLKKAKGKCPVCGRELteehrkellEEYTAELKRIEKELKEIEEK 474

                        330       340
                 ....*....|....*....|...
gi 2564278   461 KERLIKRQEELDRGYKSIMELMK 483
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIK 497
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 133-451 2.06e-06

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: 50.43  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     133 YDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 212
Cdd:TIGR00606  205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     213 SEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLsqlslEDQKRVDALNDEIRQLQQENRQLLNERIKL------- 285
Cdd:TIGR00606  285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELV-----DCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrh 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     286 -EGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEA--INKRVKDTMARSEDLDNSIDKTEAGIKELQ 362
Cdd:TIGR00606  360 qEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktAAQLCADLQSKERLKQEQADEIRDEKKGLG 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     363 KSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEA----------FEKYQTLSLKQLFRK 432
Cdd:TIGR00606  440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltetlkkevkSLQNEKADLDRKLRK 519

                          330
                   ....*....|....*....
gi 2564278     433 LEQCNTELKKYSHVNKKAL 451
Cdd:TIGR00606  520 LDQEMEQLNHHTTTRTQME 538
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-367 6.37e-06

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: 6.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    7 EPAFYTCVEVTAGNRLFYHIVDSDEVSTKILmEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDA--IPMISKLRYNPRFD 84
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAI-EYLKAAKAGRATFLPLDKIRARAALAAALARGaiGAAVDLVASDLREA 611

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   85 KAFKHVFGKTLICRSMEVSTQLARAFTMDciTLEGDQVSHRGALTGGyydtrksrlelqkdvrkaeeelgeleaklnenl 164
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAV--TLAGRLREVTLEGEGG--------------------------------- 656

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  165 rrnierinneidqlmNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKtfmpkqrsLQSLEASLHAMESTRESLKAE 244
Cdd:COG1196 657 ---------------SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAE 713

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  245 LGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNEriklEGIITRVETYLNENLRKRLDQVEQELNELretegGTV-L 323
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEE----EALEELPEPPDLEELERELERLEREIEAL-----GPVnL 784

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 2564278  324 TAtTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMER 367
Cdd:COG1196 785 LA-IEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 134-363 8.89e-06

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: 47.84  E-value: 8.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  134 DTRKSRLELQKDVRKAEEELGELEAKLNEnLRRNIERINNEIDQLMnqmQQIETQQRKFKASRDSILSEMKMLKEKRQQS 213
Cdd:COG4942  45 ALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELE---KEIAELRAELEAQKEELAELLRALYRLGRQP 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  214 EKTFMPKQRSLQSLEASLHamestreslkaelgtdLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVE 293
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQ----------------YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  294 TylnenLRKRLDQVEQELNELreteggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQK 363
Cdd:COG4942 185 E-----ERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
162-367 3.60e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSIlsemkmlkekRQQSEKTFMpkQRSLQSLEASLHAMESTRESL 241
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL----------QRLAEYSWD--EIDVASAEREIAELEAELERL 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   242 KAelgtdllsqlsleDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVEtylnenlrKRLDQVEQELNELRETEGGT 321
Cdd:COG4913  681 DA-------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------KELEQAEEELDELQDRLEAA 739

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2564278   322 VLTATTSELEAINKRVKDTMAR------SEDLDNSIDKTEAGIKELQKSMER 367
Cdd:COG4913  740 EDLARLELRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELER 791
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
206-367 4.53e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 4.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  206 LKEKRQQSEKT--FMPKQrsLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI 283
Cdd:COG3206 166 LELRREEARKAleFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  284 KLEGIITRVETYLNE--------NLRKRLDQVEQELNELRE--TEGGTVLTATTSELEAINKRVKDTMARS-EDLDNSID 352
Cdd:COG3206 244 ALRAQLGSGPDALPEllqspviqQLRAQLAELEAELAELSAryTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELE 323

                       170
                ....*....|....*
gi 2564278  353 KTEAGIKELQKSMER 367
Cdd:COG3206 324 ALQAREASLQAQLAQ 338
COG5022 COG5022
Myosin heavy chain [General function prediction only];
162-483 8.15e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 8.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEM--KMLKEKRQQSEKtfmPKQRSLQSLEASLHAMESTRE 239
Cdd:COG5022  810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFgrSLKAKKRFSLLK---KETIYLQSAQRVELAERQLQE 886

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   240 sLKAELGT-DLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-KLEGIITRVETylnENLRKRLDQVEQELNELRET 317
Cdd:COG5022  887 -LKIDVKSiSSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIaRLKKLLNNIDL---EEGPSIEYVKLPELNKLHEV 962

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   318 EGGtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH-------------MDAINHDTK 384
Cdd:COG5022  963 ESK--LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLkelpvevaelqsaSKIISSEST 1040

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   385 ELEKMTNRQ---GMLLKKKEECMKKIRELG----SLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNF 457
Cdd:COG5022 1041 ELSILKPLQklkGLLLLENNQLQARYKALKlrreNSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120

                        330       340
                 ....*....|....*....|....*.
gi 2564278   458 SEQKERLIKRQEELDRGYKSIMELMK 483
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQLVNTLEPVF 1146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 172-353 1.97e-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: 42.99  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  172 NNEIDQLMnQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLS 251
Cdd:COG1579   3 PEDLRALL-DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  252 QLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELREteggtvltATTSELE 331
Cdd:COG1579  82 LGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL-AELEAELAELEAELEEKKA--------ELDEELA 152

                       170       180
                ....*....|....*....|..
gi 2564278  332 AINKRVKDTMARSEDLDNSIDK 353
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPP 174
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 256-470 2.03e-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: 43.60  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  256 EDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRETeggtvLTATTSELEAINK 335
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAE-----LAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  336 RVKDTMARSEDLDNSIDKT-EAGIKELQKSMERWKNMEK--EHMDAIN-HDTKELEKMTNRQGMLLKKKEECMKKIRELG 411
Cdd:COG4942  98 ELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRrlQYLKYLApARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2564278  412 SLPQEAFEKYQTLSLKQLFRK--LEQCNTELKKYshvnKKALDQFVNFSEQKERLIKRQEE 470
Cdd:COG4942 178 ALLAELEEERAALEALKAERQklLARLEKELAEL----AAELAELQQEAEELEALIARLEA 234
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 174-364 2.17e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  174 EIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG------- 246
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  247 -----TDLLSQL----SLED-QKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnLRKRLDQVEQELNELRE 316
Cdd:COG3883  97 rsggsVSYLDVLlgseSFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKAELEA 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 2564278  317 TeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKS 364
Cdd:COG3883 176 Q-----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
167-412 2.51e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   167 NIERINNEIDQLMNQMQQIETQQRKFKAsrdsiLSEMKMLKEKRQQsektfmpkqrsLQSLEASLHAMESTRESLKAELG 246
Cdd:COG4913  226 AADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAA-----------ARERLAELEYLRAALRLWFAQRR 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   247 TDLLsqlsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELREteggtvltat 326
Cdd:COG4913  290 LELL-------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------- 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   327 tsELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINhdtKELEKMTNRQGMLLKKKEECMKK 406
Cdd:COG4913  353 --ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAE 427


                 ....*.
gi 2564278   407 IRELGS 412
Cdd:COG4913  428 IASLER 433
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 164-472 9.49e-04

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: 42.03  E-value: 9.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     164 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMpkqRSLQSLEASLHAMESTRESLKa 243
Cdd:pfam15921  262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAK- 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     244 ELGTDLLSQLsledQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNEnlRKRLDQVEQELNEL---RETEGG 320
Cdd:pfam15921  338 RMYEDKIEEL----EKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRlwdRDTGNS 411

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     321 TVLTATTSELEAINKRVKdtmaRSEDLDNSIDkteagiKELQKSMERwknmekeHMDAINHDTKELEKMTNRQGMLLKKK 400
Cdd:pfam15921  412 ITIDHLRRELDDRNMEVQ----RLEALLKAMK------SECQGQMER-------QMAAIQGKNESLEKVSSLTAQLESTK 474

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2564278     401 EECMKKIRELGS--LPQEAFEKY---QTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEELD 472
Cdd:pfam15921  475 EMLRKVVEELTAkkMTLESSERTvsdLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECE 551
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 199-473 9.95e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    199 ILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELG----TDLLSQLSLEDQKRVDALNDEIRQLQQE 274
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaeMDRQAAIYAEQERMAMERERELERIRQE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    275 NRQLLNERIKLEGIITRVETY-----LNENLRKRLDQVEQELNELR-----ETEGGTVLTATTSELEAI-----NKRVKD 339
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMrelerLQMERQQKNERVRQELEAARkvkilEEERQRKIQQQKVEMEQIraeqeEARQRE 436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    340 TMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEH------MDAINHDTKELEKMtnRQGMLLKKKEECMKKI----RE 409
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERkrkkleLEKEKRDRKRAEEQ--RRKILEKELEERKQAMieeeRK 514

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2564278    410 LGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHvNKKALDQFVNFSEQKERL--IKRQEELDR 473
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLeaMEREREMMR 579
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 197-284 1.14e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     197 DSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENR 276
Cdd:smart00935   7 QKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86


                   ....*...
gi 2564278     277 QLLNERIK 284
Cdd:smart00935  87 KRQQEELQ 94
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
134-348 1.26e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  134 DTRKSRLELQKDVRKAEEELGELEAKLNENLRRN-IERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQ 212
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNgLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  213 SEKT--FMPKQRSLQSLEASLHAMESTRESLKAELGtdllsqlslEDQKRVDALNDEI----RQLQQENRQLLNE-RIKL 285
Cdd:COG3206 252 GPDAlpELLQSPVIQQLRAQLAELEAELAELSARYT---------PNHPDVIALRAQIaalrAQLQQEAQRILASlEAEL 322

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2564278  286 EGIITRVETylnenLRKRLDQVEQELNELRETEggTVLTATTSELEAINKRVKDTMARSEDLD 348
Cdd:COG3206 323 EALQAREAS-----LQAQLAQLEARLAELPELE--AELRRLEREVEVARELYESLLQRLEEAR 378
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 298-473 1.30e-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: 40.90  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  298 ENLRKRLDQVEQELNELRETEggtvlTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMD 377
Cdd:COG4942  30 EQLQQEIAELEKELAALKKEE-----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  378 AINHDTKELEKMTNRQG-MLLKKKEECMKKIRELGSLpqeafeKYQTLSLKQLFRKLEQCNTELKKyshVNKKALDQFVN 456
Cdd:COG4942 105 ELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYL------KYLAPARREQAEELRADLAELAA---LRAELEAERAE 175

                       170
                ....*....|....*..
gi 2564278  457 FSEQKERLIKRQEELDR 473
Cdd:COG4942 176 LEALLAELEEERAALEA 192
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 161-413 1.36e-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: 41.16  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    161 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 240
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    241 LKAELGTDLLS----QLSLED-QKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQELNELR 315
Cdd:TIGR04523 466 LETQLKVLSRSinkiKQNLEQkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI-EKLESEKKEKESKISDLE 544

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    316 eteggtvltattSELEAINKRVKDTMARSE--DLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQ 393
Cdd:TIGR04523 545 ------------DELNKDDFELKKENLEKEidEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612

                         250       260
                  ....*....|....*....|
gi 2564278    394 GMLLKKKEECMKKIRELGSL 413
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSI 632
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
164-372 3.60e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 3.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  164 LRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKA 243
Cdd:COG4372  85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  244 ELGTDLLSQLSLEDQKRVDALNdeiRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVL 323
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALD---ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 2564278  324 TATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNME 372
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
194-316 3.88e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  194 ASRDSILSEM--KMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAElgTDLLSQLSLEDQKRVDALNDEIRQL 271
Cdd:COG2433 376 LSIEEALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE--VEELEAELEEKDERIERLERELSEA 453

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 2564278  272 QQENRQLLNERIKLEGIITRvetylNENLRKRLDQVEQELNELRE 316
Cdd:COG2433 454 RSEERREIRKDREISRLDRE-----IERLERELEEERERIEELKR 493
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 298-470 4.45e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 4.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  298 ENLRKRLDQVEQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHM- 376
Cdd:COG3883  19 QAKQKELSELQAELEAAQAE-----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAr 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278  377 ----------------------DAIN----------HDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKyqtl 424
Cdd:COG3883  94 alyrsggsvsyldvllgsesfsDFLDrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---- 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 2564278  425 sLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQEE 470
Cdd:COG3883 170 -KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 161-471 5.44e-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: 39.23  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    161 NENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRES 240
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    241 -----LKAELG------TDLLSQLSlEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLnENLRKRLDQVEQ 309
Cdd:TIGR04523 307 dwnkeLKSELKnqekklEEIQNQIS-QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI-EKLKKENQSYKQ 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    310 ELNELreteggtvltatTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKM 389
Cdd:TIGR04523 385 EIKNL------------ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    390 TNRQGMLLKKKEECMKKIRELgslpqEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKERLIKRQE 469
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVL-----SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527


                  ..
gi 2564278    470 EL 471
Cdd:TIGR04523 528 KL 529
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 162-463 5.65e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 39.65  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEmkmlkeKRQQSEKTFmpKQRSLQSLEASLHAMESTRESL 241
Cdd:TIGR01612  934 EKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLID------KINELDKAF--KDASLNDYEAKNNELIKYFNDL 1005

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     242 KAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERI-----------KLEGIITRVETYLNENLRKRLDQVEQE 310
Cdd:TIGR01612 1006 KANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIaihtsiyniidEIEKEIGKNIELLNKEILEEAEINITN 1085

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     311 LNELRETEGGTVLTATTSE-----LEAINKrVKDTMarsEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAI------ 379
Cdd:TIGR01612 1086 FNEIKEKLKHYNFDDFGKEenikyADEINK-IKDDI---KNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLedvadk 1161

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278     380 ---NHDTKELE-KMTNRQGMLLKKK---EECMKKIRELGSLP--QEAFEKYQTL------SLKQLFrkLEQCNTELKKYS 444
Cdd:TIGR01612 1162 aisNDDPEEIEkKIENIVTKIDKKKniyDEIKKLLNEIAEIEkdKTSLEEVKGInlsygkNLGKLF--LEKIDEEKKKSE 1239

                          330
                   ....*....|....*....
gi 2564278     445 HVNKKALDQFVNFSEQKER 463
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEK 1258
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-374 5.75e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   170 RINNEIDQLMNQMQQIETQQRKFKASRD-----------------SILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLH 232
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDeadevleeheerreeleTLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   233 AMESTRESLKAELGTDLLSQLSLEDQ-----KRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYlNENLRKRLDQV 307
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER-AEELREEAAEL 368

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2564278   308 EQELNELRETeggtvLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKE 374
Cdd:PRK02224 369 ESELEEAREA-----VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE 430
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-481 7.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   162 ENLRRNIERINNEIDQLMNQMQQIETQQRKFKasrdsilSEMKMLKEKRQQSEKtFMPKQRSLQSLEASLHAMESTRESL 241
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELK-------KEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   242 KAELGTdlLSQLSLEDQKRVDALND---EIRQLQQENRQLLNERIKLEgiiTRVETYlnenlrKRLDQVEQELNELRETE 318
Cdd:PRK03918 313 EKRLSR--LEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELE---ERHELY------EEAKAKKEELERLKKRL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   319 GGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNM------------EKEHMDAINHDTKEL 386
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAEL 461

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278   387 EKMTNRqgmlLKKKEECMKKIR-ELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYshvNKKALDQ-FVNFSEQKERL 464
Cdd:PRK03918 462 KRIEKE----LKEIEEKERKLRkELRELEKVLKKESELIKLKELAEQLKELEEKLKKY---NLEELEKkAEEYEKLKEKL 534

                        330
                 ....*....|....*..
gi 2564278   465 IKRQEELDRGYKSIMEL 481
Cdd:PRK03918 535 IKLKGEIKSLKKELEKL 551
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 177-393 8.05e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.88  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    177 QLMNQMQQIETQQRKFKASRDSILSEMKMLKE-KRQQSEKTfmpkqRSLQSLEASLHAM-ESTRESLKAElgtdllsqlS 254
Cdd:PRK10929  117 QLLEKSRQAQQEQDRAREISDSLSQLPQQQTEaRRQLNEIE-----RRLQTLGTPNTPLaQAQLTALQAE---------S 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564278    255 LEDQKRVDALndEIRQLQQENRQllnERIKLegiitRVETY--LNENLRKRLDQVEQELNELRETEGGTVLTATtsELEA 332
Cdd:PRK10929  183 AALKALVDEL--ELAQLSANNRQ---ELARL-----RSELAkkRSQQLDAYLQALRNQLNSQRQREAERALEST--ELLA 250

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2564278    333 INkrvkdtmarSEDLDNSIdkteagIKELQKSmerwknmeKEHMDAINHDTKELEKMTNRQ 393
Cdd:PRK10929  251 EQ---------SGDLPKSI------VAQFKIN--------RELSQALNQQAQRMDLIASQQ 288
 
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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