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Conserved domains on  [gi|670357705|ref|NP_001288246|]
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tuftelin isoform 3 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1005088)

coiled-coil domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-372 1.43e-07

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 192 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 264
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 265 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 340
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 670357705 341 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 372
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-359 2.34e-03

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


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705    31 LELYRAMCQGSVDILRLTLQGELTGDELEHIAQKAGRkTYAMVSSHSAGHSLASELveshdgheEIIKVYLKGRSGDKMI 110
Cdd:pfam15921  247 LEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQL--------EIIQEQARNQNSMYMR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   111 H----EKNINQLKSEvqyIQEARnclqKLREDISSKLDRNLgdSLHRQEIQVVLEKPNGFSQSPTALyssppevDTCINE 186
Cdd:pfam15921  318 QlsdlESTVSQLRSE---LREAK----RMYEDKIEELEKQL--VLANSELTEARTERDQFSQESGNL-------DDQLQK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   187 DVESLRKTVQDLLAKLQEAKRQHQSDcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEV-GELQRRLLGMETEHQAL 265
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESL 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   266 lakvregevaleelrsnnadcqaerekaatlekevaglrEKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE- 344
Cdd:pfam15921  461 ---------------------------------------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDl 501

                          330
                   ....*....|....*...
gi 670357705   345 ---LKEKIAYLEAENLEM 359
Cdd:pfam15921  502 tasLQEKERAIEATNAEI 519
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-372 1.43e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 192 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 264
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 265 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 340
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 670357705 341 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 372
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 186-359 2.63e-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: 49.68  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   186 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 264
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   265 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 344
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928

                          170
                   ....*....|....*
gi 670357705   345 LKEKIAYLEAENLEM 359
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 61-359 3.00e-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: 49.73  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705    61 IAQKAGRKTYAMVSSH-----SAGHSLASELVESHDGHEEIIKVYLKgrsgDKMIHEKNINQLKSEV-QYIQEARNC--- 131
Cdd:pfam15921  303 IIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYEDKIEELEK----QLVLANSELTEARTERdQFSQESGNLddq 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   132 LQKLREDISSK--------------LDRNLGDSLHRQEIQVVLEKPNGFSQSPTALYSS--------PPEVDTCINEDVE 189
Cdd:pfam15921  379 LQKLLADLHKRekelslekeqnkrlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmksecqgqMERQMAAIQGKNE 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   190 SLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQALL 266
Cdd:pfam15921  459 SLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQELQ 534

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   267 AKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNSK 332
Cdd:pfam15921  535 HLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEFK 610

                          330       340
                   ....*....|....*....|....*..
gi 670357705   333 AVIQSKDATIQELKEKIAYLEAENLEM 359
Cdd:pfam15921  611 ILKDKKDAKIRELEARVSDLELEKVKL 637
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
125-364 2.90e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 125 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 198
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 199 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 264
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 265 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 327
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 670357705 328 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 364
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 186-336 1.32e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 186 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 256
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 257 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAAtlekevaglrekihHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 336
Cdd:cd22656  189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAAL--------------RLIADLTAADTDLDNLLALIGPAIPALE 249
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-359 2.34e-03

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: 40.49  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705    31 LELYRAMCQGSVDILRLTLQGELTGDELEHIAQKAGRkTYAMVSSHSAGHSLASELveshdgheEIIKVYLKGRSGDKMI 110
Cdd:pfam15921  247 LEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQL--------EIIQEQARNQNSMYMR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   111 H----EKNINQLKSEvqyIQEARnclqKLREDISSKLDRNLgdSLHRQEIQVVLEKPNGFSQSPTALyssppevDTCINE 186
Cdd:pfam15921  318 QlsdlESTVSQLRSE---LREAK----RMYEDKIEELEKQL--VLANSELTEARTERDQFSQESGNL-------DDQLQK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   187 DVESLRKTVQDLLAKLQEAKRQHQSDcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEV-GELQRRLLGMETEHQAL 265
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESL 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   266 lakvregevaleelrsnnadcqaerekaatlekevaglrEKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE- 344
Cdd:pfam15921  461 ---------------------------------------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDl 501

                          330
                   ....*....|....*...
gi 670357705   345 ---LKEKIAYLEAENLEM 359
Cdd:pfam15921  502 tasLQEKERAIEATNAEI 519
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 192-372 1.43e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 192 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 264
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 265 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 340
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 670357705 341 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 372
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-358 1.52e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 184 INEDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 260
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 261 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 339
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        170
                 ....*....|....*....
gi 670357705 340 ATIQELKEKIAYLEAENLE 358
Cdd:COG1196  411 ALLERLERLEEELEELEEA 429
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 240-360 6.36e-07

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 51.62  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 240 RVEQ--KEAEVGELQRRLLGMETEHQALlakVREGEvaleelrsnnadcQAEREKAATLEKEVAGLREKIhhldDMLKSQ 317
Cdd:COG0542  403 RMEIdsKPEELDELERRLEQLEIEKEAL---KKEQD-------------EASFERLAELRDELAELEEEL----EALKAR 462

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 670357705 318 QRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH 360
Cdd:COG0542  463 WEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELA 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 186-359 2.63e-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: 49.68  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   186 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 264
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   265 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 344
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928

                          170
                   ....*....|....*
gi 670357705   345 LKEKIAYLEAENLEM 359
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 224-370 2.91e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 224 QREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKaatLEKEVAGL 303
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARL 300

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 670357705 304 REKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 370
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 61-359 3.00e-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: 49.73  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705    61 IAQKAGRKTYAMVSSH-----SAGHSLASELVESHDGHEEIIKVYLKgrsgDKMIHEKNINQLKSEV-QYIQEARNC--- 131
Cdd:pfam15921  303 IIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYEDKIEELEK----QLVLANSELTEARTERdQFSQESGNLddq 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   132 LQKLREDISSK--------------LDRNLGDSLHRQEIQVVLEKPNGFSQSPTALYSS--------PPEVDTCINEDVE 189
Cdd:pfam15921  379 LQKLLADLHKRekelslekeqnkrlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmksecqgqMERQMAAIQGKNE 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   190 SLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQALL 266
Cdd:pfam15921  459 SLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQELQ 534

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   267 AKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNSK 332
Cdd:pfam15921  535 HLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEFK 610

                          330       340
                   ....*....|....*....|....*..
gi 670357705   333 AVIQSKDATIQELKEKIAYLEAENLEM 359
Cdd:pfam15921  611 ILKDKKDAKIRELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 243-370 4.54e-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: 48.91  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   243 QKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREkaaTLEKEVAGLREKIHHLDDMLKSQQRKVR 322
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 670357705   323 QMIEQLQNSKAVIQSKDATIQELKEKIAYLEAE--NLEMHDRMEHLIEKQ 370
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQ 797
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-372 6.27e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 6.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   107 DKMIHEKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNlgdSLHRQEIQVVLEKPNgfsqsptalysspPEVDTcINE 186
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELE-------------AQIEQ-LKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   187 DVESLRKTVQDLLAKLQEAKR---QHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQ 263
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   264 ALLAKVREGEVALEELRSnnaDCQAEREKAATLEKEVAGLREKIHHLddmlksqqrkvRQMIEQLQNSKAVIQskdATIQ 343
Cdd:TIGR02168  877 ALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEEL-----------REKLAQLELRLEGLE---VRID 939

                          250       260
                   ....*....|....*....|....*....
gi 670357705   344 ELKEKIAYLEAENLEMHDRMEHLIEKQIS 372
Cdd:TIGR02168  940 NLQERLSEEYSLTLEEAEALENKIEDDEE 968
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-369 1.03e-05

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: 47.76  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   115 INQLKSEVQYIQEARNCLQKLREDISSKLDR-------------NLGDSLHRQEIQVVLEKPNGFSQSPTALYSSPPEVD 181
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEEleedlhkleealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   182 TCINE---DVESLRKTVQDLLAKLQEAKRQHQSDCvafevtlsryqREAEQSNVALQREEDRVEQKEAEVGELQRRLLGM 258
Cdd:TIGR02169  819 QKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIE-----------KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   259 ETEHQALLAKVREGEVALEELrsnNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQ---------RKVRQMIEQLQ 329
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEEL---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVE 964

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 670357705   330 ---------NSKAVIQSKD--ATIQELKEKIAYLEAENLEMHDRMEHLIEK 369
Cdd:TIGR02169  965 eeiralepvNMLAIQEYEEvlKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
187-382 1.14e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  187 DVESLRKTVQDLLAKLQEAKrqhqsdcvAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 266
Cdd:COG4913   662 DVASAEREIAELEAELERLD--------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  267 AKVREGEVA--------LEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLksqqrkVRQMIEQLQNSKAVIQSK 338
Cdd:COG4913   734 DRLEAAEDLarlelralLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADL 807

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 670357705  339 DATIQELKEKIAY---LEAENLEMH-DRMEHLIEKQISH--GNFSTQARA 382
Cdd:COG4913   808 DADLESLPEYLALldrLEEDGLPEYeERFKELLNENSIEfvADLLSKLRR 857
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-370 2.71e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   111 HEKNINQLKSEVQYIQEARNCLQKLREDISSKLdRNLGDSLHRQEIQVVLEKpngfsqsptalyssppevdtcinEDVES 190
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSRQISALR-----------------------KDLAR 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   191 LRKTVQdllaKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 270
Cdd:TIGR02168  738 LEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   271 EGEVALEELRSNNADCQAEREKAAT----LEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQ---NSKAVIQ------- 336
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERrledLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEealallr 893

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 670357705   337 ----SKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 370
Cdd:TIGR02168  894 seleELSEELRELESKRSELRRELEELREKLAQLELRL 931
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 234-371 4.47e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 234 LQREEDRVEQKEAEVGELQR-----------RLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKA----ATLEK 298
Cdd:COG1196  188 LERLEDILGELERQLEPLERqaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELeaelAELEA 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 670357705 299 EVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 371
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-355 9.40e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 9.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  186 EDVESLRKTVqDLLAKLQEAKRQHQ------SDCVAFEVTLSRY--QREAEQSNVALQREEDRVEQKEAEVGELQRRLLG 257
Cdd:COG4913   242 EALEDAREQI-ELLEPIRELAERYAaarerlAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  258 METEHQALLAKVRE-GEVALEELRSNNADCQAERE----KAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 332
Cdd:COG4913   321 LREELDELEAQIRGnGGDRLEQLEREIERLERELEererRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400

                         170       180
                  ....*....|....*....|....*..
gi 670357705  333 AVIQSK----DATIQELKEKIAYLEAE 355
Cdd:COG4913   401 EALEEAlaeaEAALRDLRRELRELEAE 427
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 199-392 9.99e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 199 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEE 278
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 279 LRSNNADcqAEREKA------ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYL 352
Cdd:COG1196  405 LEEAEEA--LLERLErleeelEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 670357705 353 EAENLEMHDRMEHLIEKQISHGNFSTQARAKTENPGSIRI 392
Cdd:COG1196  483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
238-386 2.21e-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: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  238 EDRVEQKEAEVGELQRRLlgmeTEHQALLAKVREGEVALEELRSNNADCQA---EREKAATLEKEVAGLREKIHHLD--- 311
Cdd:COG4913   609 RAKLAALEAELAELEEEL----AEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDass 684

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 670357705  312 DMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQARAKTEN 386
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
125-364 2.90e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 125 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 198
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 199 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 264
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 265 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 327
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 670357705 328 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 364
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
220-354 3.62e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  220 LSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG---------METEHQALLAKVREGEVALEELRSNNADCQAER 290
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSDDLAALE 691

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 670357705  291 EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQElkEKIAYLEA 354
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEE 753
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-364 3.99e-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: 42.74  E-value: 3.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   199 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR-------E 271
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   272 GEVALEELRSNNADCQAE----REKAATLEKEVAGLREKI--------------HHLDDMLKSQQRKVRQMIEQLQNSKA 333
Cdd:TIGR02168  321 LEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELeeleaeleelesrlEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190
                   ....*....|....*....|....*....|.
gi 670357705   334 VIQSKDATIQELKEKIAYLEAENLEMHDRME 364
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 186-371 4.80e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 186 EDVESLRKTVQDLLAKLQEAKRQHQSdcvaFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET---EH 262
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 263 QALLAKV-----REGEVALEELRSNNADC--------------QAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQ 323
Cdd:COG4942  103 KEELAELlralyRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 670357705 324 MIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH---DRMEHLIEKQI 371
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEALIARLE 233
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 237-369 7.51e-04

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  237 EEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDdmlkS 316
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ----S 377

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 670357705  317 QQRKVRQMIEQLQNskAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEK 369
Cdd:pfam05622 378 ELQKKKEQIEELEP--KQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEK 428
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 233-355 9.52e-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: 40.29  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 233 ALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSN------NADCQAEREKAATLEKEVAGLREK 306
Cdd:COG1579   39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealQKEIESLKRRISDLEDEILELMER 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 670357705 307 IHHLDDMLKSQQRKVRQMIEQLqnsKAVIQSKDATIQELKEKIAYLEAE 355
Cdd:COG1579  119 IEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 220-371 1.08e-03

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: 41.20  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   220 LSRYQREAEQSNvalqreedRVEQKEAEVGELQRRLLGMEtehqaLLAKVREGEVALEELRSNNADCQAEREKAATLEKE 299
Cdd:TIGR02168  202 LKSLERQAEKAE--------RYKELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 670357705   300 VAGLREKIHHLDDMLKSQQRKvrqmieqLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 371
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 186-336 1.32e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 186 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 256
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 257 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAAtlekevaglrekihHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 336
Cdd:cd22656  189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAAL--------------RLIADLTAADTDLDNLLALIGPAIPALE 249
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 186-355 1.55e-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: 40.52  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 186 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQ------------------KEAE 247
Cdd:COG4942   51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 248 VGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKihhLDDMLKSQQRKVRQMIEQ 327
Cdd:COG4942  131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKE 207

                        170       180
                 ....*....|....*....|....*...
gi 670357705 328 LQNSKAVIQSKDATIQELKEKIAYLEAE 355
Cdd:COG4942  208 LAELAAELAELQQEAEELEALIARLEAE 235
DUF1068 pfam06364
Protein of unknown function (DUF1068); This family consists of several hypothetical plant ...
 178-258 1.71e-03

Protein of unknown function (DUF1068); This family consists of several hypothetical plant proteins from Arabidopsis thaliana and Oryza sativa. The function of this family is unknown.


Pssm-ID: 399393 [Multi-domain]  Cd Length: 165  Bit Score: 38.86  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  178 PEVdtciNEDVEslrKTVQDLLA---KLQEA---KRQHQSDCVAFEV--TLSRYQREAEQSNVALQREEDRVEQKEAEVG 249
Cdd:pfam06364  72 PEV----SEEME---KNFADLLSeelKLQEAvalENQHRADMALLEAkkIASQYQKEADKCNSGMETCEEAREKAEAALV 144


                  ....*....
gi 670357705  250 ElQRRLLGM 258
Cdd:pfam06364 145 E-QRKLTAL 152
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-332 2.24e-03

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: 40.43  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   115 INQLKSEVQYIQEARNCLQKLREDISSKLDRN------LGDSLHRQE--IQVVLEKPNGFSQSPTALYSSPPEVDTcINE 186
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEekLEELKEELESLEAELEELEAELEELES-RLE 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   187 DVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEqsNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 266
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 670357705   267 AKVREGEVALEELRSNNADCQAEREKAatlEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 332
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAA---ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
184-382 2.31e-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: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 184 INEDVESLRKTVQDLLAKLQEAKRQHQSdcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRL-------- 255
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalp 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 256 -LGMETEHQALLAKVREGEVALEELRS----NNADCQAEREKAATLEK----EVAGLREKIHHLDDMLKSQQRKVRQMIE 326
Cdd:COG3206  258 eLLQSPVIQQLRAQLAELEAELAELSArytpNHPDVIALRAQIAALRAqlqqEAQRILASLEAELEALQAREASLQAQLA 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 670357705 327 QLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHL-IEKQISHGNFSTQARA 382
Cdd:COG3206  338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEArLAEALTVGNVRVIDPA 394
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 31-359 2.34e-03

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: 40.49  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705    31 LELYRAMCQGSVDILRLTLQGELTGDELEHIAQKAGRkTYAMVSSHSAGHSLASELveshdgheEIIKVYLKGRSGDKMI 110
Cdd:pfam15921  247 LEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQL--------EIIQEQARNQNSMYMR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   111 H----EKNINQLKSEvqyIQEARnclqKLREDISSKLDRNLgdSLHRQEIQVVLEKPNGFSQSPTALyssppevDTCINE 186
Cdd:pfam15921  318 QlsdlESTVSQLRSE---LREAK----RMYEDKIEELEKQL--VLANSELTEARTERDQFSQESGNL-------DDQLQK 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   187 DVESLRKTVQDLLAKLQEAKRQHQSDcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEV-GELQRRLLGMETEHQAL 265
Cdd:pfam15921  382 LLADLHKREKELSLEKEQNKRLWDRD-TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESL 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705   266 lakvregevaleelrsnnadcqaerekaatlekevaglrEKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE- 344
Cdd:pfam15921  461 ---------------------------------------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDl 501

                          330
                   ....*....|....*...
gi 670357705   345 ---LKEKIAYLEAENLEM 359
Cdd:pfam15921  502 tasLQEKERAIEATNAEI 519
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
186-355 3.47e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 186 EDVESLRKTVQDLLAKLQEAKRQHQSdcvafevtLSRYQREAEQSNVALQREEDRVEQKEA------EVGELQRRLLGME 259
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 260 TEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIhhlddmLKSQQRKVRQMIEQLQNSKAVIQSKD 339
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQ 219

                        170
                 ....*....|....*.
gi 670357705 340 ATIQELKEKIAYLEAE 355
Cdd:COG4717  220 EELEELEEELEQLENE 235
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
193-329 5.11e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 193 KTVQDLLAKLQEAKRqhqsdcvafEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELqrrllgmETEHQALLAKVREG 272
Cdd:COG2433  376 LSIEEALEELIEKEL---------PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERL-------EAEVEELEAELEEK 439

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 670357705 273 EVALEELRSNNADCQAEREKAATLEKEVAGLREKIhhldDMLKSQQRKVRQMIEQLQ 329
Cdd:COG2433  440 DERIERLERELSEARSEERREIRKDREISRLDREI----ERLERELEEERERIEELK 492
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 224-315 6.44e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 224 QREAEQSnvALQREEDRVEQKEAEvgELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGL 303
Cdd:COG0542  422 QLEIEKE--ALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497

                         90
                 ....*....|..
gi 670357705 304 REKIHHLDDMLK 315
Cdd:COG0542  498 EEELAELAPLLR 509
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
186-369 7.63e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 186 EDVESLRKTVQDLLAKLQEAKrqhqsDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQAL 265
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 266 LAKVREGEVALEElrsnnadcqaEREKAATLEKEVAGLREKIHHLDDmlksqqrkvrqmieqLQNSKAVIQSKDATIQEL 345
Cdd:PRK02224 557 REAAAEAEEEAEE----------AREEVAELNSKLAELKERIESLER---------------IRTLLAAIADAEDEIERL 611

                        170       180
                 ....*....|....*....|....
gi 670357705 346 KEKIAYLEAENLEmhdRMEHLIEK 369
Cdd:PRK02224 612 REKREALAELNDE---RRERLAEK 632
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 275-375 8.28e-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: 38.21  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 275 ALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEA 354
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100
                 ....*....|....*....|.
gi 670357705 355 ENLEMHDRMEHLIEKQISHGN 375
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGR 118
PLN02939 PLN02939
transferase, transferring glycosyl groups
 196-354 8.62e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 38.34  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 196 QDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALlakvregEVA 275
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLL-------DAS 272

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 670357705 276 LEELRSNNADCQAEREKAATLEKEVagLREKIHHLDDMLKSQQRKVRQMIEQLQNSkaviqskdatiQELKEKIAYLEA 354
Cdd:PLN02939 273 LRELESKFIVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQN-----------QDLRDKVDKLEA 338
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 112-372 8.74e-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: 38.46  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  112 EKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNlgdslHRQEIQVVLEKPNGFSQsptaLYSSPPEVDTcINEDVESL 191
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT-----QTQLNQLKDEQNKIKKQ----LSEKQKELEQ-NNKKIKEL 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  192 RKTVQDLLAKLQEAKRQHQSDCV-AFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 270
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705  271 EGEVALEELRSNNadcQAEREKAATLEKEVAGLREKIHH-------LDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQ 343
Cdd:TIGR04523 367 EKQNEIEKLKKEN---QSYKQEIKNLESQINDLESKIQNqeklnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443

                         250       260
                  ....*....|....*....|....*....
gi 670357705  344 ELKEKIAYLEAENLEMHDRMEHLiEKQIS 372
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESL-ETQLK 471
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
238-356 9.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670357705 238 EDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQ 317
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 670357705 318 QRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAEN 356
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
 
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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