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Conserved domains on  [gi|767910378|ref|XP_011508263|]
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tuftelin isoform X3 [Homo sapiens]

Protein Classification

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]; ...
 114-294 2.26e-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: 52.25  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 114 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 186
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 187 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 262
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767910378 263 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 294
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-294 2.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 114 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 186
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 187 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 262
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767910378 263 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 294
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 108-281 3.80e-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: 48.53  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   108 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   187 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 266
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928

                          170
                   ....*....|....*
gi 767910378   267 LKEKIAYLEAENLEM 281
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 111-281 5.44e-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: 48.19  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   111 ESLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQAL 187
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   188 LAKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNS 253
Cdd:pfam15921  534 QHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEF 609

                          170       180
                   ....*....|....*....|....*...
gi 767910378   254 KAVIQSKDATIQELKEKIAYLEAENLEM 281
Cdd:pfam15921  610 KILKDKKDAKIRELEARVSDLELEKVKL 637
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
47-286 6.82e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  47 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 120
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 187 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 249
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767910378 250 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 286
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 108-271 3.91e-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: 38.50  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 108 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 178
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 179 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAATlekevagLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 258
Cdd:cd22656  189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAALR-------LIADLTAADTDLDNLLALIGPAIPALEKLQGAWQ 256

                        170
                 ....*....|...
gi 767910378 259 SKDATIQELKEKI 271
Cdd:cd22656  257 AIATDLDSLKDLL 269
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 114-294 2.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 114 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 186
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 187 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 262
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767910378 263 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 294
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 106-280 2.39e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 106 INEDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 182
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 183 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 261
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        170
                 ....*....|....*....
gi 767910378 262 ATIQELKEKIAYLEAENLE 280
Cdd:COG1196  411 ALLERLERLEEELEELEEA 429
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 162-282 4.95e-07

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 51.24  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 162 RVEQ--KEAEVGELQRRLLGMETEHQALlakVREGEvaleelrsnnadcQAEREKAATLEKEVAGLREKIhhldDMLKSQ 239
Cdd:COG0542  403 RMEIdsKPEELDELERRLEQLEIEKEAL---KKEQD-------------EASFERLAELRDELAELEEEL----EALKAR 462

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767910378 240 QRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH 282
Cdd:COG0542  463 WEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELA 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 108-281 3.80e-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: 48.53  E-value: 3.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   108 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   187 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 266
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928

                          170
                   ....*....|....*
gi 767910378   267 LKEKIAYLEAENLEM 281
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-292 3.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 146 QREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKaatLEKEVAGL 225
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARL 300

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767910378 226 REKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 292
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 111-281 5.44e-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: 48.19  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   111 ESLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQAL 187
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   188 LAKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNS 253
Cdd:pfam15921  534 QHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEF 609

                          170       180
                   ....*....|....*....|....*...
gi 767910378   254 KAVIQSKDATIQELKEKIAYLEAENLEM 281
Cdd:pfam15921  610 KILKDKKDAKIRELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 165-292 6.44e-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: 47.76  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   165 QKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREkaaTLEKEVAGLREKIHHLDDMLKSQQRKVR 244
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 767910378   245 QMIEQLQNSKAVIQSKDATIQELKEKIAYLEAE--NLEMHDRMEHLIEKQ 292
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQ 797
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 34-294 1.82e-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: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378    34 EKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNLGD-SLHRQEIQVVLEKPNGFSQSPTALYSSPPEVDTCINEdVES 112
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEE 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   113 LRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG------------- 179
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedie 855

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   180 ---------------METEHQALLAKVREGEVALEELRSnnaDCQAEREKAATLEKEVAGLREKIHHLddmlksqqrkvR 244
Cdd:TIGR02168  856 slaaeieeleelieeLESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEEL-----------R 921

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 767910378   245 QMIEQLQNSKAVIQskdATIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 294
Cdd:TIGR02168  922 EKLAQLELRLEGLE---VRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 37-291 2.75e-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: 45.83  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378    37 INQLKSEVQYIQEARNCLQKLREDISSKLDR-------------NLGDSLHRQEIQVVLEKPNGFSQSPTALYSSPPEVD 103
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEEleedlhkleealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   104 TCINE---DVESLRKTVQDLLAKLQEAKRQHQSDCvafevtlsryqREAEQSNVALQREEDRVEQKEAEVGELQRRLLGM 180
Cdd:TIGR02169  819 QKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIE-----------KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   181 ETEHQALLAKVREGEVALEELrsnNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQ---------RKVRQMIEQLQ 251
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEEL---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVE 964

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767910378   252 ---------NSKAVIQSKD--ATIQELKEKIAYLEAENLEMHDRMEHLIEK 291
Cdd:TIGR02169  965 eeiralepvNMLAIQEYEEvlKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-304 2.92e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  109 DVESLRKTVQDLLAKLQEAKrqhqsdcvAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 188
Cdd:COG4913   662 DVASAEREIAELEAELERLD--------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  189 AKVREGEVA--------LEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLksqqrkVRQMIEQLQNSKAVIQSK 260
Cdd:COG4913   734 DRLEAAEDLarlelralLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADL 807

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767910378  261 DATIQELKEKIAY---LEAENLEMH-DRMEHLIEKQISH--GNFSTQARA 304
Cdd:COG4913   808 DADLESLPEYLALldrLEEDGLPEYeERFKELLNENSIEfvADLLSKLRR 857
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 156-293 6.97e-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: 6.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 156 LQREEDRVEQKEAEVGELQR-----------RLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKA----ATLEK 220
Cdd:COG1196  188 LERLEDILGELERQLEPLERqaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELeaelAELEA 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767910378 221 EVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 293
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-292 7.67e-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: 44.66  E-value: 7.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378    33 HEKNINQLKSEVQYIQEARNCLQKLREDISSKLdRNLGDSLHRQEIQVVLEKpngfsqsptalyssppevdtcinEDVES 112
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSRQISALR-----------------------KDLAR 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   113 LRKTVQdllaKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 192
Cdd:TIGR02168  738 LEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   193 EGEVALEELRSNNADCQAEREKAAT----LEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQ---NSKAVIQ------- 258
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERrledLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEealallr 893

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 767910378   259 ----SKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 292
Cdd:TIGR02168  894 seleELSEELRELESKRSELRRELEELREKLAQLELRL 931
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 121-314 1.39e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEE 200
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 201 LRSNNADcqAEREKA------ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYL 274
Cdd:COG1196  405 LEEAEEA--LLERLErleeelEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767910378 275 EAENLEMHDRMEHLIEKQISHGNFSTQARAKTENPGSIRI 314
Cdd:COG1196  483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-277 2.01e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  108 EDVESLRKTVqDLLAKLQEAKRQHQ------SDCVAFEVTLSRY--QREAEQSNVALQREEDRVEQKEAEVGELQRRLLG 179
Cdd:COG4913   242 EALEDAREQI-ELLEPIRELAERYAaarerlAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  180 METEHQALLAKVRE-GEVALEELRSNNADCQAERE----KAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 254
Cdd:COG4913   321 LREELDELEAQIRGnGGDRLEQLEREIERLERELEererRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400

                         170       180
                  ....*....|....*....|....*..
gi 767910378  255 AVIQSK----DATIQELKEKIAYLEAE 277
Cdd:COG4913   401 EALEEAlaeaEAALRDLRRELRELEAE 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
160-308 3.86e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  160 EDRVEQKEAEVGELQRRLlgmeTEHQALLAKVREGEVALEELRSNNADCQA---EREKAATLEKEVAGLREKIHHLD--- 233
Cdd:COG4913   609 RAKLAALEAELAELEEEL----AEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDass 684

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767910378  234 DMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQARAKTEN 308
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
142-276 5.83e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  142 LSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG---------METEHQALLAKVREGEVALEELRSNNADCQAER 212
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSDDLAALE 691

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767910378  213 EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQElkEKIAYLEA 276
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEE 753
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
47-286 6.82e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  47 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 120
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 187 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 249
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767910378 250 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 286
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-286 8.34e-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: 41.20  E-value: 8.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR-------E 193
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   194 GEVALEELRSNNADCQAE----REKAATLEKEVAGLREKI--------------HHLDDMLKSQQRKVRQMIEQLQNSKA 255
Cdd:TIGR02168  321 LEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELeeleaeleelesrlEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190
                   ....*....|....*....|....*....|.
gi 767910378   256 VIQSKDATIQELKEKIAYLEAENLEMHDRME 286
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
DUF1068 pfam06364
Protein of unknown function (DUF1068); This family consists of several hypothetical plant ...
 100-180 8.49e-04

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: 39.63  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  100 PEVdtciNEDVEslrKTVQDLLA---KLQEA---KRQHQSDCVAFEV--TLSRYQREAEQSNVALQREEDRVEQKEAEVG 171
Cdd:pfam06364  72 PEV----SEEME---KNFADLLSeelKLQEAvalENQHRADMALLEAkkIASQYQKEADKCNSGMETCEEAREKAEAALV 144


                  ....*....
gi 767910378  172 ElQRRLLGM 180
Cdd:pfam06364 145 E-QRKLTAL 152
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 159-291 9.54e-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: 40.83  E-value: 9.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378  159 EEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDdmlkS 238
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ----S 377

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767910378  239 QQRKVRQMIEQLQNskAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEK 291
Cdd:pfam05622 378 ELQKKKEQIEELEP--KQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEK 428
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-293 1.42e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 108 EDVESLRKTVQDLLAKLQEAKRQHQSdcvaFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET---EH 184
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 185 QALLAKV-----REGEVALEELRSNNADC--------------QAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQ 245
Cdd:COG4942  103 KEELAELlralyRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767910378 246 MIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH---DRMEHLIEKQI 293
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEALIARLE 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-293 2.05e-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: 40.04  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   142 LSRYQREAEQSNvalqreedRVEQKEAEVGELQRRLLGMEtehqaLLAKVREGEVALEELRSNNADCQAEREKAATLEKE 221
Cdd:TIGR02168  202 LKSLERQAEKAE--------RYKELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767910378   222 VAGLREKIHHLDDMLKSQQRKvrqmieqLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 293
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 155-277 2.10e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 155 ALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSN------NADCQAEREKAATLEKEVAGLREK 228
Cdd:COG1579   39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealQKEIESLKRRISDLEDEILELMER 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767910378 229 IHHLDDMLKSQQRKVRQMIEQLqnsKAVIQSKDATIQELKEKIAYLEAE 277
Cdd:COG1579  119 IEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAE 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 108-277 3.16e-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: 38.98  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 108 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQ------------------KEAE 169
Cdd:COG4942   51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 170 VGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKihhLDDMLKSQQRKVRQMIEQ 249
Cdd:COG4942  131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKE 207

                        170       180
                 ....*....|....*....|....*...
gi 767910378 250 LQNSKAVIQSKDATIQELKEKIAYLEAE 277
Cdd:COG4942  208 LAELAAELAELQQEAEELEALIARLEAE 235
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
106-304 3.55e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 106 INEDVESLRKTVQDLLAKLQEAKRQHQSdcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRL-------- 177
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalp 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 178 -LGMETEHQALLAKVREGEVALEELRS----NNADCQAEREKAATLEK----EVAGLREKIHHLDDMLKSQQRKVRQMIE 248
Cdd:COG3206  258 eLLQSPVIQQLRAQLAELEAELAELSArytpNHPDVIALRAQIAALRAqlqqEAQRILASLEAELEALQAREASLQAQLA 337

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767910378 249 QLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHL-IEKQISHGNFSTQARA 304
Cdd:COG3206  338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEArLAEALTVGNVRVIDPA 394
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 108-271 3.91e-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: 38.50  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 108 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 178
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 179 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAATlekevagLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 258
Cdd:cd22656  189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAALR-------LIADLTAADTDLDNLLALIGPAIPALEKLQGAWQ 256

                        170
                 ....*....|...
gi 767910378 259 SKDATIQELKEKI 271
Cdd:cd22656  257 AIATDLDSLKDLL 269
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 37-254 4.65e-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: 38.88  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378    37 INQLKSEVQYIQEARNCLQKLREDISSKLDRN------LGDSLHRQE--IQVVLEKPNGFSQSPTALYSSPPEVDTcINE 108
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEekLEELKEELESLEAELEELEAELEELES-RLE 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   109 DVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEqsNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 188
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767910378   189 AKVREGEVALEELRSNNADCQAEREKAatlEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 254
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAA---ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
144-251 5.56e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 144 RYQREAEQSNVALQREEDRVEQKEAEVGELqrrllgmETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVA 223
Cdd:COG2433  396 EAEREKEHEERELTEEEEEIRRLEEQVERL-------EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS 468

                         90       100
                 ....*....|....*....|....*...
gi 767910378 224 GLREKIhhldDMLKSQQRKVRQMIEQLQ 251
Cdd:COG2433  469 RLDREI----ERLERELEEERERIEELK 492
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 146-237 5.66e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.52  E-value: 5.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 146 QREAEQSnvALQREEDRVEQKEAEvgELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGL 225
Cdd:COG0542  422 QLEIEKE--ALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497

                         90
                 ....*....|..
gi 767910378 226 REKIHHLDDMLK 237
Cdd:COG0542  498 EEELAELAPLLR 509
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 110-281 5.91e-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: 38.56  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   110 VESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTL------------SRYQREAEQSNV--ALQREEDRVEQKEAEVG---E 172
Cdd:pfam15921  319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselteartERDQFSQESGNLddQLQKLLADLHKREKELSlekE 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378   173 LQRRLLGMETEHQALLAKVREG------EVALEE--LRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVR 244
Cdd:pfam15921  399 QNKRLWDRDTGNSITIDHLRRElddrnmEVQRLEalLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767910378   245 QMIEQLQNSKAVIQSKDATIQE----LKEKIAYLEAENLEM 281
Cdd:pfam15921  479 KVVEELTAKKMTLESSERTVSDltasLQEKERAIEATNAEI 519
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
108-277 7.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 108 EDVESLRKTVQDLLAKLQEAKRQHQSdcvafevtLSRYQREAEQSNVALQREEDRVEQKEA------EVGELQRRLLGME 181
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 182 TEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIhhlddmLKSQQRKVRQMIEQLQNSKAVIQSKD 261
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQ 219

                        170
                 ....*....|....*.
gi 767910378 262 ATIQELKEKIAYLEAE 277
Cdd:COG4717  220 EELEELEEELEQLENE 235
PLN02939 PLN02939
transferase, transferring glycosyl groups
 118-276 7.75e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 37.96  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767910378 118 QDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALlakvregEVA 197
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLL-------DAS 272

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767910378 198 LEELRSNNADCQAEREKAATLEKEVagLREKIHHLDDMLKSQQRKVRQMIEQLQNSkaviqskdatiQELKEKIAYLEA 276
Cdd:PLN02939 273 LRELESKFIVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQN-----------QDLRDKVDKLEA 338
 
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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