NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19075340|ref|NP_587840|]
View 

CASP domain-containing family protein [Schizosaccharomyces pombe]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1008275)

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CASP_C super family cl24206
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ...
 404-621 7.39e-38

CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.


The actual alignment was detected with superfamily member pfam08172:

Pssm-ID: 462392 [Multi-domain]  Cd Length: 247  Bit Score: 140.88  E-value: 7.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   404 KKASFLEQKASEQEEVIRKLEKDLADVDVEGSVY--------LSNTTYRREGTSGQLSPTSSIMGGNPSlfngsvlsRNS 475
Cdd:pfam08172   4 EELSSLNAELEEQQELNAKLENDLLKVQDEASNAfsfndassAGSGVSRYPPSGGRRSPTSSIISGFEP--------SES 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   476 VNETGSAIVDVIKQQRDRFRRANVTLVNQVSAANDKIALLESKLEEVEKSNTLLYEQMRFRDHYQK-------------- 541
Cdd:pfam08172  76 SSSSDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRgggggtksssstss 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   542 -----HVEPSSSHLQTA----AAYENSISPFASFRKKEAERAYSRMGSFERIVYALLRTLLFSRATRGLFFMYLILLHLF 612
Cdd:pfam08172 156 sasayGNNPNPSDVEALdkyrKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLL 235


                  ....*....
gi 19075340   613 IMIVLLKLG 621
Cdd:pfam08172 236 VFFTLYYVS 244
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-428 5.37e-09

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 5.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    117 LKTQKQIEDLKKEKEEMEGSLQGKEK----LEREVENLRKELDKyKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQ 192
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKalaeLRKELEELEEELEQ-LRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    193 ENAsTIQKLTSKIRELQA--SQLDHDLQASQNESAGLDvnaksAEVNAILSELDDANKIIVELQAEIAVLKQN--TKEQK 268
Cdd:TIGR02168  752 LSK-ELTELEAEIEELEErlEEAEEELAEAEAEIEELE-----AQIEQLKEELKALREALDELRAELTLLNEEaaNLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    269 SGSSQDDLSNQQKqQLDFMDSLNKKLSTELESIkEASRKEMETHCATIQTLENEVKEARKVKEESLTLANkfSDYDEIKR 348
Cdd:TIGR02168  826 LESLERRIAATER-RLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLR--SELEELSE 901

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    349 ELSVLkqiefsgEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQE--------SKKASFLEQKASEQEEVI 420
Cdd:TIGR02168  902 ELREL-------ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRL 974


                   ....*...
gi 19075340    421 RKLEKDLA 428
Cdd:TIGR02168  975 KRLENKIK 982
 
Name Accession Description Interval E-value
CASP_C pfam08172
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ...
 404-621 7.39e-38

CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.


Pssm-ID: 462392 [Multi-domain]  Cd Length: 247  Bit Score: 140.88  E-value: 7.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   404 KKASFLEQKASEQEEVIRKLEKDLADVDVEGSVY--------LSNTTYRREGTSGQLSPTSSIMGGNPSlfngsvlsRNS 475
Cdd:pfam08172   4 EELSSLNAELEEQQELNAKLENDLLKVQDEASNAfsfndassAGSGVSRYPPSGGRRSPTSSIISGFEP--------SES 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   476 VNETGSAIVDVIKQQRDRFRRANVTLVNQVSAANDKIALLESKLEEVEKSNTLLYEQMRFRDHYQK-------------- 541
Cdd:pfam08172  76 SSSSDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRgggggtksssstss 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   542 -----HVEPSSSHLQTA----AAYENSISPFASFRKKEAERAYSRMGSFERIVYALLRTLLFSRATRGLFFMYLILLHLF 612
Cdd:pfam08172 156 sasayGNNPNPSDVEALdkyrKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLL 235


                  ....*....
gi 19075340   613 IMIVLLKLG 621
Cdd:pfam08172 236 VFFTLYYVS 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-428 5.37e-09

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: 59.69  E-value: 5.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    117 LKTQKQIEDLKKEKEEMEGSLQGKEK----LEREVENLRKELDKyKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQ 192
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKalaeLRKELEELEEELEQ-LRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    193 ENAsTIQKLTSKIRELQA--SQLDHDLQASQNESAGLDvnaksAEVNAILSELDDANKIIVELQAEIAVLKQN--TKEQK 268
Cdd:TIGR02168  752 LSK-ELTELEAEIEELEErlEEAEEELAEAEAEIEELE-----AQIEQLKEELKALREALDELRAELTLLNEEaaNLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    269 SGSSQDDLSNQQKqQLDFMDSLNKKLSTELESIkEASRKEMETHCATIQTLENEVKEARKVKEESLTLANkfSDYDEIKR 348
Cdd:TIGR02168  826 LESLERRIAATER-RLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLR--SELEELSE 901

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    349 ELSVLkqiefsgEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQE--------SKKASFLEQKASEQEEVI 420
Cdd:TIGR02168  902 ELREL-------ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRL 974


                   ....*...
gi 19075340    421 RKLEKDLA 428
Cdd:TIGR02168  975 KRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-439 7.62e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 7.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 131 EEMEGSLqgkEKLEREVENLRKeldkYKDLVETEAEKRAAIT---KEECEKSWLEQQKLYKDMEQENASTIQKLTSKIRE 207
Cdd:COG1196 196 GELERQL---EPLERQAEKAER----YRELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 208 LQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEQKsgSSQDDLSNQQKQQLDFM 287
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--EELEELEEELEELEEEL 346

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 288 DSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDYDEIKRELSVLKQIEfsgEHATHEN 367
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEEL 423

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075340 368 TSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDLADVDVEGSVYLS 439
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 9-444 4.82e-07

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: 53.20  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340      9 LQKLTESWKNSRFEELQREADEAAAEIEKMQKTSlDERKELSSKTKEFRKQPDEVKLGEMKglLKLYQSGIDSLTKRAKS 88
Cdd:pfam15921  431 LEALLKAMKSECQGQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMT--LESSERTVSDLTASLQE 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340     89 AEATFFRVYETLGEVPDPYPLLIEAANNLKTQ-KQIEDLKKEKEEMEGSLQGKEKLereVENLRKELDKYKDLVETEAEK 167
Cdd:pfam15921  508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKV---IEILRQQIENMTQLVGQHGRT 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    168 RAAItkeECEKSWLEQQKLYKDME-QENASTIQKLTSKIRELQASQLDHDLQASQNESAGLD----VNAKSAEVNAILSE 242
Cdd:pfam15921  585 AGAM---QVEKAQLEKEINDRRLElQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIKQERDQLLNE 661

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    243 LDDANKIIVELQAEIAVLKQNTKEQKSgsSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEAS----------RKEMETH 312
Cdd:pfam15921  662 VKTSRNELNSLSEDYEVLKRNFRNKSE--EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmQKQITAK 739

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    313 CATIQTLENEVKearkVKEESLTLANKFSDYdeIKRELSVLKQiEFSGEHATHENTSLESQLLK-REKQLSEELAKLRST 391
Cdd:pfam15921  740 RGQIDALQSKIQ----FLEEAMTNANKEKHF--LKEEKNKLSQ-ELSTVATEKNKMAGELEVLRsQERRLKEKVANMEVA 812

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 19075340    392 naqlTDRITQESKKASFLEQKaSEQEEVIRKLEKDLADVDVEGSVYLSNTTYR 444
Cdd:pfam15921  813 ----LDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKELQGPGYTSNSSMK 860
PTZ00121 PTZ00121
MAEBL; Provisional
 39-432 8.34e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    39 QKTSLDERKELSSKTKEFRKQPDEVKLGEmkgLLKLYQSGIDSLTKRAKSAEATFFRVYETLGEVPDPYPLLIEAANNLK 118
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEE---VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   119 TQKQIEDLKKEKEEMEGSlqgKEKLEREVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQENASTI 198
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   199 QKlTSKIRELQASQLDHDLQASQNESAGLDVNaksaevnailselDDANKIIVELQAEIAVLKQNTKEQKSGSSQDDLSN 278
Cdd:PTZ00121 1722 KK-AEEENKIKAEEAKKEAEEDKKKAEEAKKD-------------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   279 QQKQQLDFMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDYDEIKRELSVL---KQ 355
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnKE 1867

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   356 IEFSGEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLT----DRITQESKKASFLEQKASE-QEEVIRKLEKDLADV 430
Cdd:PTZ00121 1868 ADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgknnDIIDDKLDKDEYIKRDAEEtREEIIKISKKDMCIN 1947


                  ..
gi 19075340   431 DV 432
Cdd:PTZ00121 1948 DF 1949
 
Name Accession Description Interval E-value
CASP_C pfam08172
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ...
 404-621 7.39e-38

CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.


Pssm-ID: 462392 [Multi-domain]  Cd Length: 247  Bit Score: 140.88  E-value: 7.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   404 KKASFLEQKASEQEEVIRKLEKDLADVDVEGSVY--------LSNTTYRREGTSGQLSPTSSIMGGNPSlfngsvlsRNS 475
Cdd:pfam08172   4 EELSSLNAELEEQQELNAKLENDLLKVQDEASNAfsfndassAGSGVSRYPPSGGRRSPTSSIISGFEP--------SES 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   476 VNETGSAIVDVIKQQRDRFRRANVTLVNQVSAANDKIALLESKLEEVEKSNTLLYEQMRFRDHYQK-------------- 541
Cdd:pfam08172  76 SSSSDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRgggggtksssstss 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   542 -----HVEPSSSHLQTA----AAYENSISPFASFRKKEAERAYSRMGSFERIVYALLRTLLFSRATRGLFFMYLILLHLF 612
Cdd:pfam08172 156 sasayGNNPNPSDVEALdkyrKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLL 235


                  ....*....
gi 19075340   613 IMIVLLKLG 621
Cdd:pfam08172 236 VFFTLYYVS 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-428 5.37e-09

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: 59.69  E-value: 5.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    117 LKTQKQIEDLKKEKEEMEGSLQGKEK----LEREVENLRKELDKyKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQ 192
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKalaeLRKELEELEEELEQ-LRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    193 ENAsTIQKLTSKIRELQA--SQLDHDLQASQNESAGLDvnaksAEVNAILSELDDANKIIVELQAEIAVLKQN--TKEQK 268
Cdd:TIGR02168  752 LSK-ELTELEAEIEELEErlEEAEEELAEAEAEIEELE-----AQIEQLKEELKALREALDELRAELTLLNEEaaNLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    269 SGSSQDDLSNQQKqQLDFMDSLNKKLSTELESIkEASRKEMETHCATIQTLENEVKEARKVKEESLTLANkfSDYDEIKR 348
Cdd:TIGR02168  826 LESLERRIAATER-RLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNERASLEEALALLR--SELEELSE 901

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    349 ELSVLkqiefsgEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQE--------SKKASFLEQKASEQEEVI 420
Cdd:TIGR02168  902 ELREL-------ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALENKIEDDEEEARRRL 974


                   ....*...
gi 19075340    421 RKLEKDLA 428
Cdd:TIGR02168  975 KRLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-433 1.00e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 1.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    120 QKQIEDLKKEKEEMEGSL----QGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKE---------ECEKSWLEQQKL 186
Cdd:TIGR02168  711 EEELEQLRKELEELSRQIsalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeelaEAEAEIEELEAQ 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    187 YKDMEQENASTIQKLTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAvlKQNTKE 266
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE--ELEELI 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    267 QKSGSSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEASRKemethcatIQTLENEVKEAR-KVKEESLTLANKFSDYDE 345
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESK--------RSELRRELEELReKLAQLELRLEGLEVRIDN 940

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    346 IKRELSVLKQIEFSGEHATHENTSLESQLLKRE-KQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLE 424
Cdd:TIGR02168  941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020


                   ....*....
gi 19075340    425 KDLADVDVE 433
Cdd:TIGR02168 1021 EAIEEIDRE 1029
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 143-427 1.42e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    143 LEREVENLRKELDK---YKDLVETEAEKRAAIT---KEECEKSWLEQQKLYKDMEQEnastIQKLTSKIRELQASQLDHD 216
Cdd:TIGR02168  198 LERQLKSLERQAEKaerYKELKAELRELELALLvlrLEELREELEELQEELKEAEEE----LEELTAELQELEEKLEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    217 LQASQNESAgldVNAKSAEVNAILSELDDANKIIVELQAEIAVLkQNTKEQKSGSSQDDLSNQQKQQLDFmdSLNKKLST 296
Cdd:TIGR02168  274 LEVSELEEE---IEELQKELYALANEISRLEQQKQILRERLANL-ERQLEELEAQLEELESKLDELAEEL--AELEEKLE 347

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    297 ELESIKEASRKEMETHCATIQTLENEVKEARkvkEESLTLAnkfSDYDEIKRELSV----LKQIEFSGEHATHENTSLES 372
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELE---EQLETLR---SKVAQLELQIASlnneIERLEARLERLEDRRERLQQ 421

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075340    373 QLLKREKQLSE-ELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDL 427
Cdd:TIGR02168  422 EIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-439 7.62e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 7.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 131 EEMEGSLqgkEKLEREVENLRKeldkYKDLVETEAEKRAAIT---KEECEKSWLEQQKLYKDMEQENASTIQKLTSKIRE 207
Cdd:COG1196 196 GELERQL---EPLERQAEKAER----YRELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 208 LQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEQKsgSSQDDLSNQQKQQLDFM 287
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE--EELEELEEELEELEEEL 346

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 288 DSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDYDEIKRELSVLKQIEfsgEHATHEN 367
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL---ERLEEEL 423

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075340 368 TSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDLADVDVEGSVYLS 439
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 125-433 3.62e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.53  E-value: 3.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    125 DLKKEK--EEMEGSLQGKEKLEREVENLRKELDKYKDLVEtEAEKRAAITKEECEKSWLEQQKLYKDMEQEnastIQKLT 202
Cdd:TIGR02169  169 DRKKEKalEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYELLKEKEALERQ----KEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    203 SKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKI-----IVELQAEIAVLKQNTKEQKSgsSQDDLS 277
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkekIGELEAEIASLERSIAEKER--ELEDAE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    278 NQQKQQLDFMDslnkklstELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLT-LANKFSDYDEIKRELSVLKQi 356
Cdd:TIGR02169  322 ERLAKLEAEID--------KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFAETRDELKDYRE- 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    357 efSGEHATHENTSLE---SQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDLADVDVE 433
Cdd:TIGR02169  393 --KLEKLKREINELKrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 9-444 4.82e-07

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: 53.20  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340      9 LQKLTESWKNSRFEELQREADEAAAEIEKMQKTSlDERKELSSKTKEFRKQPDEVKLGEMKglLKLYQSGIDSLTKRAKS 88
Cdd:pfam15921  431 LEALLKAMKSECQGQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMT--LESSERTVSDLTASLQE 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340     89 AEATFFRVYETLGEVPDPYPLLIEAANNLKTQ-KQIEDLKKEKEEMEGSLQGKEKLereVENLRKELDKYKDLVETEAEK 167
Cdd:pfam15921  508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEgDHLRNVQTECEALKLQMAEKDKV---IEILRQQIENMTQLVGQHGRT 584

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    168 RAAItkeECEKSWLEQQKLYKDME-QENASTIQKLTSKIRELQASQLDHDLQASQNESAGLD----VNAKSAEVNAILSE 242
Cdd:pfam15921  585 AGAM---QVEKAQLEKEINDRRLElQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIKQERDQLLNE 661

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    243 LDDANKIIVELQAEIAVLKQNTKEQKSgsSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEAS----------RKEMETH 312
Cdd:pfam15921  662 VKTSRNELNSLSEDYEVLKRNFRNKSE--EMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkvamgmQKQITAK 739

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    313 CATIQTLENEVKearkVKEESLTLANKFSDYdeIKRELSVLKQiEFSGEHATHENTSLESQLLK-REKQLSEELAKLRST 391
Cdd:pfam15921  740 RGQIDALQSKIQ----FLEEAMTNANKEKHF--LKEEKNKLSQ-ELSTVATEKNKMAGELEVLRsQERRLKEKVANMEVA 812

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 19075340    392 naqlTDRITQESKKASFLEQKaSEQEEVIRKLEKDLADVDVEGSVYLSNTTYR 444
Cdd:pfam15921  813 ----LDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKELQGPGYTSNSSMK 860
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 57-410 2.25e-06

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: 50.84  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340     57 RKQPDEV-----KLGEMKGLLKLYQSGIDSLTKRAKSAEATFFRVYETLGEVPDPYPLLIEAANnlKTQKQIEDLKKEKE 131
Cdd:TIGR02169  670 RSEPAELqrlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE--KLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    132 EMEgslQGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQENASTIQKLTSKIRELQAS 211
Cdd:TIGR02169  748 SLE---QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    212 QLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKqnTKEQKSGSSQDDLSNQQKQQLDFMDSLN 291
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE--AALRDLESRLGDLKKERDELEAQLRELE 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    292 KKLStELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDYDEIK-------RELSVLKQIEFSGEHAT 364
Cdd:TIGR02169  903 RKIE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQaelqrveEEIRALEPVNMLAIQEY 981

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 19075340    365 HEntslesqLLKREKQLSEELAKLRSTNAQLTDRI--TQESKKASFLE 410
Cdd:TIGR02169  982 EE-------VLKRLDELKEKRAKLEEERKAILERIeeYEKKKREVFME 1022
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 114-526 7.81e-06

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: 49.35  E-value: 7.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    114 ANNLKTQKQIedlKKEKEEMEGSLQGKE--KLEREVENLRKELDK----YKDLVEtEAEKRAAITKEECEKSWLEQQKLy 187
Cdd:pfam15921  294 ANSIQSQLEI---IQEQARNQNSMYMRQlsDLESTVSQLRSELREakrmYEDKIE-ELEKQLVLANSELTEARTERDQF- 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    188 kdmEQENASTIQKLTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANkiiVELQAEIAVLKQNTKEQ 267
Cdd:pfam15921  369 ---SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRN---MEVQRLEALLKAMKSEC 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    268 KSGSSQDDLSNQQKQQldfmdSLNK--KLSTELESIKEASRKEMETHCATIQTLEN----------EVKEARKVKEESLT 335
Cdd:pfam15921  443 QGQMERQMAAIQGKNE-----SLEKvsSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltaSLQEKERAIEATNA 517

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    336 LANKFSDYDEIK-RELSVLKQIEFSGEHATHENTSLESQLLKREK------QLSEELAKL-----------RSTNAQLTD 397
Cdd:pfam15921  518 EITKLRSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAEKDKvieilrQQIENMTQLvgqhgrtagamQVEKAQLEK 597

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    398 RITQESKKASFLEQKASEQEEVIRKLEKDLADVDVEgSVYLSNTTYRRegtsgqLSPTSSIMGGNPSLFNGSVLSRNSVN 477
Cdd:pfam15921  598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELE-KVKLVNAGSER------LRAVKDIKQERDQLLNEVKTSRNELN 670

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 19075340    478 ETGSAIVDVIKQQRDRFRRANVT---LVNQVSAANDKIALLESKLEEVEKSN 526
Cdd:pfam15921  671 SLSEDYEVLKRNFRNKSEEMETTtnkLKMQLKSAQSELEQTRNTLKSMEGSD 722
PTZ00121 PTZ00121
MAEBL; Provisional
 39-432 8.34e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    39 QKTSLDERKELSSKTKEFRKQPDEVKLGEmkgLLKLYQSGIDSLTKRAKSAEATFFRVYETLGEVPDPYPLLIEAANNLK 118
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEE---VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   119 TQKQIEDLKKEKEEMEGSlqgKEKLEREVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQENASTI 198
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   199 QKlTSKIRELQASQLDHDLQASQNESAGLDVNaksaevnailselDDANKIIVELQAEIAVLKQNTKEQKSGSSQDDLSN 278
Cdd:PTZ00121 1722 KK-AEEENKIKAEEAKKEAEEDKKKAEEAKKD-------------EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   279 QQKQQLDFMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDYDEIKRELSVL---KQ 355
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnKE 1867

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   356 IEFSGEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLT----DRITQESKKASFLEQKASE-QEEVIRKLEKDLADV 430
Cdd:PTZ00121 1868 ADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgknnDIIDDKLDKDEYIKRDAEEtREEIIKISKKDMCIN 1947


                  ..
gi 19075340   431 DV 432
Cdd:PTZ00121 1948 DF 1949
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 183-429 8.42e-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: 48.61  E-value: 8.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 183 QQKLYKDMEQENASTIQKLTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQ 262
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 263 NTKEQKsgssqddlsNQQKQQLDFMDSLNKKLSTEL----ESIKEASRKEMethcatiqtLENEVKEARKVKEEsltlan 338
Cdd:COG4942  98 ELEAQK---------EELAELLRALYRLGRQPPLALllspEDFLDAVRRLQ---------YLKYLAPARREQAE------ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 339 kfsdydEIKRELSVLKQIEFSGEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEE 418
Cdd:COG4942 154 ------ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                       250
                ....*....|.
gi 19075340 419 VIRKLEKDLAD 429
Cdd:COG4942 228 LIARLEAEAAA 238
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
123-354 3.24e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 3.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  123 IEDLKKEKEEMEGSLQGKEKLEREVENLRKELDKYKDLveteaEKRAAITKEECEKSWLEQQKLYKDMEQENASTIQKLT 202
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL-----KKKLAELEKKLDELEEELAELLKELEELGFESVEELE 591

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  203 SKIRELQaSQLDHDLQASQNESaglDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEQKSGSSQDDLSNQQKQ 282
Cdd:PRK03918 592 ERLKELE-PFYNEYLELKDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE 667

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075340  283 QLDfMDSLNKKLSTELESIKEaSRKEMEthcATIQTLENEVKEARKVKEESLTLANKFSDYDEIKRELSVLK 354
Cdd:PRK03918 668 YLE-LSRELAGLRAELEELEK-RREEIK---KTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 115-424 4.73e-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: 46.55  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   115 NNLKTQKQIED----LKKEKEEMEGSLQGKEKLEREVENLRKELDKYKdlvETEAEKRAAITKEECEKSWLEQQ-KLYKD 189
Cdd:TIGR04523 357 ENSEKQRELEEkqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQE---KLNQQKDEQIKKLQQEKELLEKEiERLKE 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   190 MEQENASTIQKLTSKIRELQASQLDHDLQASQNESaglDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEqks 269
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE--- 507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   270 gssqddLSNQQKQQLDFMDSLNKKLStELESikEASRKEMEthcatIQTLENEVKEarkvKEESLTLANKFSDYDEIKRE 349
Cdd:TIGR04523 508 ------LEEKVKDLTKKISSLKEKIE-KLES--EKKEKESK-----ISDLEDELNK----DDFELKKENLEKEIDEKNKE 569

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075340   350 LSVLKqiefsgehatHENTSLEsqllKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLE 424
Cdd:TIGR04523 570 IEELK----------QTQKSLK----KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
PRK12704 PRK12704
phosphodiesterase; Provisional
 121-207 5.61e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  121 KQIEDLKKEKEEMEGSLQGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQKlyKDMEQENASTIQK 200
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVE--EEARHEAAVLIKE 177


                 ....*..
gi 19075340  201 LTSKIRE 207
Cdd:PRK12704 178 IEEEAKE 184
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 124-395 6.13e-05

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: 46.27  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   124 EDLKKEKEEMEGSLQGKEKLEREVENLRKELDKyKDLVETEAEKRAAITKEECEKSWLEQQKlyKDMEQENASTIQKLTS 203
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEIS 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   204 KIRELQASQLD---------HDLQAS-----QNESAGLDVNAKSAEVNAILSELDDANKIIV------------------ 251
Cdd:pfam17380 376 RMRELERLQMErqqknervrQELEAArkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVrrleeeraremervrlee 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   252 -ELQAEIAVLKQNTKEQKSGSSQDDLSNQQKQQLDfmDSLNKKLSTELESIKEA------SRKEMETHCATIQTLENEVK 324
Cdd:pfam17380 456 qERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE--EQRRKILEKELEERKQAmieeerKRKLLEKEMEERQKAIYEEE 533

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075340   325 EARKVKEESLTlankfsdydeiKRELSVLKQIEFSGEHATHENTSLESqlLKREKQLSEELAKLRSTNAQL 395
Cdd:pfam17380 534 RRREAEEERRK-----------QQEMEERRRIQEQMRKATEERSRLEA--MEREREMMRQIVESEKARAEY 591
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 115-427 8.11e-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: 45.78  E-value: 8.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   115 NNLKTQKQIEDLKKEKEEMEGSLQGKEKLEREVENLRKELDKykdlveteaekraaiTKEECEKSWLEQQKLYKDMEQEN 194
Cdd:TIGR04523  94 NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKE---------------NKKNIDKFLTEIKKKEKELEKLN 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   195 aSTIQKLTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLK-QNTKEQKSGSSQ 273
Cdd:TIGR04523 159 -NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKkQNNQLKDNIEKK 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   274 DDLSNQQKQQLDFMDSLNKKLSTELESIK---EASRKEMETHCATI-------QTLENEVKEARKVKEESLT------LA 337
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKkqlSEKQKELEQNNKKIkelekqlNQLKSEISDLNNQKEQDWNkelkseLK 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   338 NKFSDYDEIKRELS-----------VLKQIEFSGEHATHENTSLESQLLKREKqlseELAKLRSTNAQLTDRITQESKKA 406
Cdd:TIGR04523 318 NQEKKLEEIQNQISqnnkiisqlneQISQLKKELTNSESENSEKQRELEEKQN----EIEKLKKENQSYKQEIKNLESQI 393

                         330       340
                  ....*....|....*....|.
gi 19075340   407 SFLEQKASEQEEVIRKLEKDL 427
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQI 414
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 118-436 1.03e-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: 45.40  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   118 KTQKQIEDLKKEKEEMEGSLQGK----EKLEREVENLRKELDKYK-DLVETEAEKRAAITKEEceKSWLEQQKLYKDMEQ 192
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKqkelEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKEL--KSELKNQEKKLEEIQ 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   193 ENASTIQKLTSKIRElQASQLDHDLQASQNESAGLD--VNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEQKSG 270
Cdd:TIGR04523 328 NQISQNNKIISQLNE-QISQLKKELTNSESENSEKQreLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   271 SSQDDLSNQQKQQldfMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSD-YDEIKRE 349
Cdd:TIGR04523 407 NQQKDEQIKKLQQ---EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsINKIKQN 483

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   350 LSVLKQiEFSgehathENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDLAD 429
Cdd:TIGR04523 484 LEQKQK-ELK------SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556


                  ....*..
gi 19075340   430 VDVEGSV 436
Cdd:TIGR04523 557 ENLEKEI 563
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-339 1.72e-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: 44.37  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 138 QGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKE--ECEKSWLEQQKLYKDMEQENAST---IQKLTSKIRELQAS- 211
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAEl 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 212 ---------QLDHDLQASQNESAGLDVNAKS-------------------AEVNAILSELDDANKIIVELQAEIAVLKQN 263
Cdd:COG4942 100 eaqkeelaeLLRALYRLGRQPPLALLLSPEDfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAELEAL 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075340 264 TKEQKsgSSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEASRKEmETHCATIQTLENEVKEARKVKEESLTLANK 339
Cdd:COG4942 180 LAELE--EERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALK 252
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 196-417 1.75e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 196 STIQKLTSKIRELQAsqldhDLQASQNESAGLD--VNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKE------- 266
Cdd:COG3883  16 PQIQAKQKELSELQA-----ELEAAQAELDALQaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelge 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 267 -----QKSGSSQDDLSN--QQKQQLDFMDSLNKklsteLESIKEASRKEMETHCATIQTLENEVKEARKVKEEsltLANK 339
Cdd:COG3883  91 raralYRSGGSVSYLDVllGSESFSDFLDRLSA-----LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEAL 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075340 340 FSDYDEIKRELsvlkqiefsgEHATHENTSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQE 417
Cdd:COG3883 163 KAELEAAKAEL----------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-268 1.96e-04

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: 44.66  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340      6 EALLQKLTESwkNSRFEELQREAdeaaaeiekmqktsldERKELSSKTKEFRKQPDEVKLGEMKGLLKLYQSGIDSLTKR 85
Cdd:TIGR02168  242 EELQEELKEA--EEELEELTAEL----------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340     86 AKSAEATFFRVYETLGEVpdpypllieAANNLKTQKQIEDLKKEKEEMEgslQGKEKLEREVENLRKELDKYKDLVEtEA 165
Cdd:TIGR02168  304 KQILRERLANLERQLEEL---------EAQLEELESKLDELAEELAELE---EKLEELKEELESLEAELEELEAELE-EL 370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    166 EKRAaitkEECEKSWLEQQKLYKDMEQEnastIQKLTSKIREL--QASQLDHDLQASQNESAGLDVNAKSAEVNAILSEL 243
Cdd:TIGR02168  371 ESRL----EELEEQLETLRSKVAQLELQ----IASLNNEIERLeaRLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442

                          250       260
                   ....*....|....*....|....*
gi 19075340    244 DDANKIIVELQAEIAVLKQNTKEQK 268
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELR 467
PRK11281 PRK11281
mechanosensitive channel MscK;
117-433 2.13e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   117 LKTQKQIEDLKKEKEEMEGSLQGkekLEREVENLRKELDKYKDLVETEAEKR-AAITKEECEKSWLE----QQKLYKDME 191
Cdd:PRK11281   69 LALLDKIDRQKEETEQLKQQLAQ---APAKLRQAQAELEALKDDNDEETRETlSTLSLRQLESRLAQtldqLQNAQNDLA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   192 QENASTIQKLTSKIReLQAsQLDHDLQASQnesagldvnaksaEVNAILSELDDANKII-----VELQAEIAVLK-QNTK 265
Cdd:PRK11281  146 EYNSQLVSLQTQPER-AQA-ALYANSQRLQ-------------QIRNLLKGGKVGGKALrpsqrVLLQAEQALLNaQNDL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   266 EQKSGSSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEA-SRKEMEthcatiQTlENEVKEArkvkeESLTLANKFSDYD 344
Cdd:PRK11281  211 QRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAiNSKRLT------LS-EKTVQEA-----QSQDEAARIQANP 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   345 EIKRELSVLKQIEFSGEHATHENTSLESQ----------LLKREKQLSEELAKLRSTnaQLTDRITQEskkasflEQKAS 414
Cdd:PRK11281  279 LVAQELEINLQLSQRLLKATEKLNTLTQQnlrvknwldrLTQSERNIKEQISVLKGS--LLLSRILYQ-------QQQAL 349

                         330
                  ....*....|....*....
gi 19075340   415 EQEEVIRKLEKDLADVDVE 433
Cdd:PRK11281  350 PSADLIEGLADRIADLRLE 368
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 42-325 2.31e-04

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: 44.65  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340     42 SLDERKELSSKTKEFRKQPDEvkLGEMKGLLKLYQSGIDSLTKRAKSAEATFFRVYETLGEV----PDPYPLLIEAANNL 117
Cdd:TIGR00606  634 SQDEESDLERLKEEIEKSSKQ--RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELqefiSDLQSKLRLAPDKL 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    118 K-TQKQIEDLKKEKEEMEGSLQGK----EKLEREVENLRKELDKYK--------DLVETEAEKRAAITKEECEKSWLEQQ 184
Cdd:TIGR00606  712 KsTESELKKKEKRRDEMLGLAPGRqsiiDLKEKEIPELRNKLQKVNrdiqrlknDIEEQETLLGTIMPEEESAKVCLTDV 791

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    185 KLYKDMEQENASTIQKLTSKIRELQASQLDHDLQASQNEsagldVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNT 264
Cdd:TIGR00606  792 TIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE-----KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075340    265 KEQKSGSSQDDLSNQQKQQldfMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKE 325
Cdd:TIGR00606  867 NELKSEKLQIGTNLQRRQQ---FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 110-223 2.54e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.05  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  110 LIEAAnnlktQKQIEDLKKEKEEMEGSLQGKEK-LE---REVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQK 185
Cdd:PRK00409 503 IIEEA-----KKLIGEDKEKLNELIASLEELEReLEqkaEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 19075340  186 LYKDMEQENASTIQKLTSKIRELQASQLDHDLQASQNE 223
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR 615
PRK12704 PRK12704
phosphodiesterase; Provisional
 297-427 2.72e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  297 ELESIKEASRKEMETHcatiqtleneVKEA-RKVKEESLTLANKFsdYDEIKRELSVLKQiefsgehathentsLESQLL 375
Cdd:PRK12704  39 EAKRILEEAKKEAEAI----------KKEAlLEAKEEIHKLRNEF--EKELRERRNELQK--------------LEKRLL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19075340  376 KREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLEKDL 427
Cdd:PRK12704  93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
120-453 2.89e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  120 QKQIEDLKKEKEEMEGSLQGKEKLEREVENLRKELDKYKDLVETEAE------KRAAITKEECEKSWLEQQKLYKDMEQE 193
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkRLTGLTPEKLEKELEELEKAKEEIEEE 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  194 nastIQKLTSKIRELQASQLDHDLQASQNESAgldvNAKSAEVNAILSELDDANkIIVELQAEIAVLKQNTKEQKSGSSQ 273
Cdd:PRK03918 407 ----ISKITARIGELKKEIKELKKAIEELKKA----KGKCPVCGRELTEEHRKE-LLEEYTAELKRIEKELKEIEEKERK 477

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  274 ddlSNQQKQQLDFMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLTLANKFSDydeIKRELSVL 353
Cdd:PRK03918 478 ---LRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS---LKKELEKL 551

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  354 KQIEfsgehatHENTSLESQLLKREKQLSEELAKLR----STNAQLTDRITQ-ESKKASFLEQKASEQE-EVIRKLEKDL 427
Cdd:PRK03918 552 EELK-------KKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKElEPFYNEYLELKDAEKElEREEKELKKL 624

                        330       340
                 ....*....|....*....|....*.
gi 19075340  428 ADVDVEGSVYLSNTTYRREGTSGQLS 453
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELE 650
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
44-430 9.83e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   44 DERKELSSKTKEFRKQPDEVKlgEMKGLLKLYQSGIDSLTKRAKSAEatffrvyETLGEvpdpypllieaannlkTQKQI 123
Cdd:PRK03918 214 SELPELREELEKLEKEVKELE--ELKEEIEELEKELESLEGSKRKLE-------EKIRE----------------LEERI 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  124 EDLKKEKEEME---GSLQGKEKLEREVENLRKELDKYKDlVETEAEKRAAITKEECEkswlEQQKLYKDMEQENaSTIQK 200
Cdd:PRK03918 269 EELKKEIEELEekvKELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRLEEEIN----GIEERIKELEEKE-ERLEE 342

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  201 LTSKIRELQ--------ASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAVLKQNTKEQKSgss 272
Cdd:PRK03918 343 LKKKLKELEkrleeleeRHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK--- 419

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  273 qddLSNQQKQQLDFMDSLNKKLSTELESIKEASRKE-METHCATIQTLENEVKEA----RKVKEESLTLANKFSDYDEIK 347
Cdd:PRK03918 420 ---EIKELKKAIEELKKAKGKCPVCGRELTEEHRKElLEEYTAELKRIEKELKEIeekeRKLRKELRELEKVLKKESELI 496

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  348 RELSVLKQIEFSGEhathentSLESQLLKREKQLSEELAKLRSTNAQLTDRIT---QESKKASFLEQKASEQEEVIRKLE 424
Cdd:PRK03918 497 KLKELAEQLKELEE-------KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKslkKELEKLEELKKKLAELEKKLDELE 569


                 ....*.
gi 19075340  425 KDLADV 430
Cdd:PRK03918 570 EELAEL 575
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
43-425 1.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   43 LDERKELSSKTKEFRKQPDEV--KLGEMKGLLKLYQ------SGIDSLTKRAK-----SAEATFFRVYETLGEVPDPYPL 109
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELekRLEELEERHELYEeakakkEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISK 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  110 LIEAANNLKTQ-----KQIEDLKKEK-----------EEMEGSLqgKEKLEREVENLRKELDKYKdlvetEAEKRAAITK 173
Cdd:PRK03918 410 ITARIGELKKEikelkKAIEELKKAKgkcpvcgreltEEHRKEL--LEEYTAELKRIEKELKEIE-----EKERKLRKEL 482

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  174 EECEKSWLEQQKLYKdmEQENASTIQKLTSKIRELQASQLDHDLQASQNesagldVNAKSAEVNAILSELDDANKIIVEL 253
Cdd:PRK03918 483 RELEKVLKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAEEYEK------LKEKLIKLKGEIKSLKKELEKLEEL 554

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  254 QAEIAVLkqntkEQKSGSSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEASRKEMETHCAT--IQTLENEVK-EARKVK 330
Cdd:PRK03918 555 KKKLAEL-----EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEkeLEREEKELKkLEEELD 629

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  331 EESLTLANKFSDYDEIKRELSVLKQIEFSGEHATHENTSLEsqllkrekqLSEELAKLRSTNAQLTDRITQESKKASFLE 410
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE---------LSRELAGLRAELEELEKRREEIKKTLEKLK 700

                        410
                 ....*....|....*
gi 19075340  411 QKASEQEEVIRKLEK 425
Cdd:PRK03918 701 EELEEREKAKKELEK 715
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 116-354 1.61e-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: 41.54  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   116 NLKTQKQIEDLKKEKEEMEGSLQGKEKLEREVENLRKELDK----YKDLVETEAEKRAAITKEECEKSWLEQQ-----KL 186
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseIKDLTNQDSVKELIIKNLDNTRESLETQlkvlsRS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   187 YKDMEQENASTIQKLTSKIREL-----QASQLDHDLQ--ASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAv 259
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELkklneEKKELEEKVKdlTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK- 555

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   260 lKQNTKEQKSGSSQ--DDLSNQQKQQLDFMDSLNKKLStELESIKEASRKEMETHCATIQTLENEVKEARKVKEE-SLTL 336
Cdd:TIGR04523 556 -KENLEKEIDEKNKeiEELKQTQKSLKKKQEEKQELID-QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKlSSII 633

                         250
                  ....*....|....*...
gi 19075340   337 ANKFSDYDEIKRELSVLK 354
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIK 651
PTZ00121 PTZ00121
MAEBL; Provisional
 22-425 1.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    22 EELQREADEAAAEIEKMQKTSLDERKELSSKTKEFRKQPDEVKLGEMKG-LLKLYQSGIDSLTKRAKSAEATFFRVYETL 100
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   101 GEVPDPYPLLIEAANNLKTQKQIEDLKKEKEEMEGSLQGKEKLE--REVENLRKELDKYKDLVETEAEKRAAITKEECEK 178
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   179 SWLEQQKlyKDMEQENASTIQKLTSKIRELQASQLDHDlQASQNESAGLDVNAKSAEVNAILSELDDANKI--IVEL-QA 255
Cdd:PTZ00121 1478 KAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkADELkKA 1554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   256 EIAVLKQNTKEQKSGSSQDDLSNQQKQQLDFMDSLNKKLSTELESIKEASRKEMETHCATIQTLENEVKEARKVKEESLT 335
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340   336 LANKFSDYDEIKRELSVLKQIEfsgehatHENTSLESQLLKR---EKQLSEELAKLRSTNAQLTDRITQESKKASFLEQK 412
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAE-------EENKIKAAEEAKKaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707

                         410
                  ....*....|...
gi 19075340   413 ASEQEEVIRKLEK 425
Cdd:PTZ00121 1708 KKKEAEEKKKAEE 1720
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 121-332 1.78e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    121 KQIEDLKKEkeemegslqgKEKLEREVENLRKELDKYKDLVEtEAEKRAAITKEEcekswleqqklYKDMEQEnastIQK 200
Cdd:TIGR02169  343 REIEEERKR----------RDKLTEEYAELKEELEDLRAELE-EVDKEFAETRDE-----------LKDYREK----LEK 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340    201 LTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKiivELQAEIAvlkqnTKEQKSGSSQDDLSNQQ 280
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE---DKALEIK-----KQEWKLEQLAADLSKYE 468

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 19075340    281 KQQLDFMDSLNKklsteLESIKEASRKEMETHCATIQTLENEVKEARKVKEE 332
Cdd:TIGR02169  469 QELYDLKEEYDR-----VEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
PLN02939 PLN02939
transferase, transferring glycosyl groups
 119-415 1.99e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.43  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  119 TQKQIEDLKKEK----EEMEGSLQGKEKLEREVENLRKELDKYKDLVETEAEKRAAItkeECEKSWLEqqKLYKDMEQEN 194
Cdd:PLN02939 140 AEKNILLLNQARlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHV---EILEEQLE--KLRNELLIRG 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  195 ASTIQKLTSKIRELqasqldhDLQASQNESAGLDVNAKSAEvnaiLSELDDANKIIVELQAEIAVLKQNTKEQKSG--SS 272
Cdd:PLN02939 215 ATEGLCVHSLSKEL-------DVLKEENMLLKDDIQFLKAE----LIEVAETEERVFKLEKERSLLDASLRELESKfiVA 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  273 QDDLSNQQKQQldfMDSLNKKLSTeLESIKEASRKEMETHCATI---QTLENEVKEArkvkEESLTLAN--KFSDY--DE 345
Cdd:PLN02939 284 QEDVSKLSPLQ---YDCWWEKVEN-LQDLLDRATNQVEKAALVLdqnQDLRDKVDKL----EASLKEANvsKFSSYkvEL 355

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  346 IKRELSVLKQIEFSGEHATHENTSLESQLLkreKQLSEELAKLRstnaqltdritQESKKASfLEQKASE 415
Cdd:PLN02939 356 LQQKLKLLEERLQASDHEIHSYIQLYQESI---KEFQDTLSKLK-----------EESKKRS-LEHPADD 410
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
192-424 3.51e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 192 QENASTIQKLTSKIRELQA--SQLDHDLQASQNESAGLDVnakSAEVNAILSELDDANKIIVELQAEIAVLKQNtkeqks 269
Cdd:COG3206 171 EEARKALEFLEEQLPELRKelEEAEAALEEFRQKNGLVDL---SEEAKLLLQQLSELESQLAEARAELAEAEAR------ 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 270 gssqddlsnqqkqqldfMDSLNKKLSTELESIKEASRKemethcATIQTLENEVKEAR-KVKEESLTLANKFSDYDEIKR 348
Cdd:COG3206 242 -----------------LAALRAQLGSGPDALPELLQS------PVIQQLRAQLAELEaELAELSARYTPNHPDVIALRA 298

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19075340 349 ELSVLKQiefsgehathentSLESQLLKREKQLSEELAKLRSTNAQLTDRITQESKKASFLEQKASEQEEVIRKLE 424
Cdd:COG3206 299 QIAALRA-------------QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
43-428 4.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  43 LDERKELSSKTKEFRKQPDEVKlgEMKGLLKLYQSGIDSLTKRAKSAEATFfRVYETLGEVPDPYPLLIEAANNLKT-QK 121
Cdd:COG4717  70 LKELKELEEELKEAEEKEEEYA--ELQEELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELAElPE 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 122 QIEDLKKEKEEMEGSLQGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKEECEKSWLEQQKLYKDMEQENAsTIQKL 201
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE-ELEEL 225

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 202 TSKIRELQASQLDHDLQASQNE--------SAGLDVNAKSAEVNAILSELDDANKIIVELQAeIAVLKQNTKEQKSGSSQ 273
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEarlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-LLFLLLAREKASLGKEA 304

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 274 DDLSN-------QQKQQLDFMDSLNKKLSTELESIKEASR--KEMETHCATIQTLENE--VKEARKVKEESLTLAN---- 338
Cdd:COG4717 305 EELQAlpaleelEEEELEELLAALGLPPDLSPEELLELLDriEELQELLREAEELEEElqLEELEQEIAALLAEAGvede 384

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 339 --------KFSDYDEIKRELSVLKQ------IEFSGEHATHENTSLESQLL----------KREKQLSEELAKLRSTNAQ 394
Cdd:COG4717 385 eelraaleQAEEYQELKEELEELEEqleellGELEELLEALDEEELEEELEeleeeleeleEELEELREELAELEAELEQ 464

                       410       420       430
                ....*....|....*....|....*....|....
gi 19075340 395 LtdritQESKKASFLEQKASEQEEVIRKLEKDLA 428
Cdd:COG4717 465 L-----EEDGELAELLQELEELKAELRELAEEWA 493
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
119-424 6.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  119 TQKQIEDLKkekEEMEGSLQGKEKLEREVENLRKELDKYKDLVETEAEKRAAITKE------ECEKSWLEQQKLYKDMEQ 192
Cdd:PRK02224 249 RREELETLE---AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddaDAEAVEARREELEDRDEE 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  193 ------ENASTIQKLTSKIRELQASQLDHDLQAS--QNESAGLDVNAKSAEvnailSELDDANKIIVELQAEIAVLkqnt 264
Cdd:PRK02224 326 lrdrleECRVAAQAHNEEAESLREDADDLEERAEelREEAAELESELEEAR-----EAVEDRREEIEELEEEIEEL---- 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  265 kEQKSGSSQDDLSNQQkqqlDFMDslnkklstELESIKEASRKEMETHCATIQTLENEVKEARKVKE-----------ES 333
Cdd:PRK02224 397 -RERFGDAPVDLGNAE----DFLE--------ELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvEG 463

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  334 LTLANKFSDYDEIKRELSV-LKQIEFSGEHATHENTSLES---------QLLKREKQLSEELAKLRSTNAQLTDRITQES 403
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAeLEDLEEEVEEVEERLERAEDlveaedrieRLEERREDLEELIAERRETIEEKRERAEELR 543

                        330       340
                 ....*....|....*....|.
gi 19075340  404 KKASFLEQKASEQEEVIRKLE 424
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAE 564
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-283 6.16e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340  20 RFEELQREADEAAAEIEKMQKTSLDERKELSSKTKEFRkqpdevklgEMKGLLKLYQSGIDSLTKRAKSAEATffrvyet 99
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEY---------ELLAELARLEQDIARLEERRRELEER------- 317

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 100 lgevpdpypLLIEAANNLKTQKQIEDLKKEKEEMEGSLQGKEKLEREVENLRKEldkykdlvETEAEKRAAITKEECEKS 179
Cdd:COG1196 318 ---------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE--------AEEALLEAEAELAEAEEE 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075340 180 WLEQQKLYKDMEQENASTIQKLTSKIRELQASQLDHDLQASQNESAGLDVNAKSAEVNAILSELDDANKIIVELQAEIAV 259
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                       250       260
                ....*....|....*....|....
gi 19075340 260 LKQNTKEQKSGSSQDDLSNQQKQQ 283
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLE 484
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH