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Conserved domains on  [gi|119573814|gb|EAW53429|]
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tuftelin 1, isoform CRA_a [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]; ...
173-353 1.83e-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: 53.40  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 173 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 245
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 246 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 321
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                        170       180       190
                 ....*....|....*....|....*....|..
gi 119573814 322 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 353
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
173-353 1.83e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 173 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 245
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 246 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 321
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                        170       180       190
                 ....*....|....*....|....*....|..
gi 119573814 322 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 353
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
42-340 2.28e-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: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814    42 IAQKAGRKTYAMVSSH-----SAGHSLASELVESHDGHEEIIKVYLKgrsgDKMIHEKNINQLKSEV-QYIQEARNC--- 112
Cdd:pfam15921  303 IIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYEDKIEELEK----QLVLANSELTEARTERdQFSQESGNLddq 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   113 LQKLREDISSK--------------LDRNLGDSLHRQEIQVVLEKPNGFSQSPTALYSS--------PPEVDTCINEDVE 170
Cdd:pfam15921  379 LQKLLADLHKRekelslekeqnkrlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmksecqgqMERQMAAIQGKNE 458
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   171 SLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQALL 247
Cdd:pfam15921  459 SLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQELQ 534
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   248 AKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNSK 313
Cdd:pfam15921  535 HLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEFK 610
                          330       340
                   ....*....|....*....|....*..
gi 119573814   314 AVIQSKDATIQELKEKIAYLEAENLEM 340
Cdd:pfam15921  611 ILKDKKDAKIRELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
167-340 2.90e-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: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   167 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 245
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   246 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 325
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          170
                   ....*....|....*
gi 119573814   326 LKEKIAYLEAENLEM 340
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
106-345 4.55e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 106 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 179
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 180 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 245
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 246 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 308
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119573814 309 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 345
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
167-317 3.17e-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: 39.28  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 167 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 237
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 238 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAAtlekevaglrekihHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 317
Cdd:cd22656  189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAAL--------------RLIADLTAADTDLDNLLALIGPAIPALE 249
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
173-353 1.83e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 173 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 245
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 246 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 321
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                        170       180       190
                 ....*....|....*....|....*....|..
gi 119573814 322 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 353
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
165-339 2.00e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 165 INEDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 241
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 242 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 320
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                        170
                 ....*....|....*....
gi 119573814 321 ATIQELKEKIAYLEAENLE 339
Cdd:COG1196  411 ALLERLERLEEELEELEEA 429
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
221-341 7.06e-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: 7.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 221 RVEQ--KEAEVGELQRRLLGMETEHQALlakVREGEvaleelrsnnadcQAEREKAATLEKEVAGLREKIhhldDMLKSQ 298
Cdd:COG0542  403 RMEIdsKPEELDELERRLEQLEIEKEAL---KKEQD-------------EASFERLAELRDELAELEEEL----EALKAR 462
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 119573814 299 QRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH 341
Cdd:COG0542  463 WEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELA 505
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
42-340 2.28e-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: 2.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814    42 IAQKAGRKTYAMVSSH-----SAGHSLASELVESHDGHEEIIKVYLKgrsgDKMIHEKNINQLKSEV-QYIQEARNC--- 112
Cdd:pfam15921  303 IIQEQARNQNSMYMRQlsdleSTVSQLRSELREAKRMYEDKIEELEK----QLVLANSELTEARTERdQFSQESGNLddq 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   113 LQKLREDISSK--------------LDRNLGDSLHRQEIQVVLEKPNGFSQSPTALYSS--------PPEVDTCINEDVE 170
Cdd:pfam15921  379 LQKLLADLHKRekelslekeqnkrlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmksecqgqMERQMAAIQGKNE 458
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   171 SLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQALL 247
Cdd:pfam15921  459 SLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQELQ 534
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   248 AKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNSK 313
Cdd:pfam15921  535 HLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEFK 610
                          330       340
                   ....*....|....*....|....*..
gi 119573814   314 AVIQSKDATIQELKEKIAYLEAENLEM 340
Cdd:pfam15921  611 ILKDKKDAKIRELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
167-340 2.90e-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: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   167 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 245
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   246 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 325
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          170
                   ....*....|....*
gi 119573814   326 LKEKIAYLEAENLEM 340
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-351 3.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 205 QREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKaatLEKEVAGL 284
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARL 300
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119573814 285 REKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 351
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
224-351 5.15e-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: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   224 QKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREkaaTLEKEVAGLREKIHHLDDMLKSQQRKVR 303
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 119573814   304 QMIEQLQNSKAVIQSKDATIQELKEKIAYLEAE--NLEMHDRMEHLIEKQ 351
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQ 797
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
88-353 9.39e-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: 47.74  E-value: 9.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814    88 DKMIHEKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNlgdSLHRQEIQVVLEKPNgfsqsptalysspPEVDTcINE 167
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELE-------------AQIEQ-LKE 796
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   168 DVESLRKTVQDLLAKLQEAKR---QHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQ 244
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   245 ALLAKVREGEVALEELRSnnaDCQAEREKAATLEKEVAGLREKIHHLddmlksqqrkvRQMIEQLQNSKAVIQskdATIQ 324
Cdd:TIGR02168  877 ALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEEL-----------REKLAQLELRLEGLE---VRID 939
                          250       260
                   ....*....|....*....|....*....
gi 119573814   325 ELKEKIAYLEAENLEMHDRMEHLIEKQIS 353
Cdd:TIGR02168  940 NLQERLSEEYSLTLEEAEALENKIEDDEE 968
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
96-350 1.20e-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: 47.37  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814    96 INQLKSEVQYIQEARNCLQKLREDISSKLDR-------------NLGDSLHRQEIQVVLEKPNGFSQSPTALYSSPPEVD 162
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEEleedlhkleealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   163 TCINE---DVESLRKTVQDLLAKLQEAKRQHQSDCvafevtlsryqREAEQSNVALQREEDRVEQKEAEVGELQRRLLGM 239
Cdd:TIGR02169  819 QKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIE-----------KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   240 ETEHQALLAKVREGEVALEELrsnNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQ---------RKVRQMIEQLQ 310
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEEL---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVE 964
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 119573814   311 ---------NSKAVIQSKD--ATIQELKEKIAYLEAENLEMHDRMEHLIEK 350
Cdd:TIGR02169  965 eeiralepvNMLAIQEYEEvlKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
168-363 2.29e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  168 DVESLRKTVQDLLAKLQEAKrqhqsdcvAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 247
Cdd:COG4913   662 DVASAEREIAELEAELERLD--------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  248 AKVREGEVA--------LEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLksqqrkVRQMIEQLQNSKAVIQSK 319
Cdd:COG4913   734 DRLEAAEDLarlelralLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADL 807
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 119573814  320 DATIQELKEKIAY---LEAENLEMH-DRMEHLIEKQISH--GNFSTQARA 363
Cdd:COG4913   808 DADLESLPEYLALldrLEEDGLPEYeERFKELLNENSIEfvADLLSKLRR 857
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-351 4.07e-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: 45.82  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814    92 HEKNINQLKSEVQYIQEARNCLQKLREDISSKLdRNLGDSLHRQEIQVVLEKpngfsqsptalyssppevdtcinEDVES 171
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSRQISALR-----------------------KDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   172 LRKTVQdllaKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 251
Cdd:TIGR02168  738 LEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   252 EGEVALEELRSNNADCQAEREKAAT----LEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQ---NSKAVIQ------- 317
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERrledLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEealallr 893
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 119573814   318 ----SKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 351
Cdd:TIGR02168  894 seleELSEELRELESKRSELRRELEELREKLAQLELRL 931
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
215-352 5.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 215 LQREEDRVEQKEAEVGELQR-----------RLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKA----ATLEK 279
Cdd:COG1196  188 LERLEDILGELERQLEPLERqaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELeaelAELEA 267
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119573814 280 EVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 352
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
180-373 1.17e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 180 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEE 259
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 260 LRSNNADcqAEREKA------ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYL 333
Cdd:COG1196  405 LEEAEEA--LLERLErleeelEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 119573814 334 EAENLEMHDRMEHLIEKQISHGNFSTQARAKTENPGSIRI 373
Cdd:COG1196  483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
167-336 1.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  167 EDVESLRKTVqDLLAKLQEAKRQHQ------SDCVAFEVTLSRY--QREAEQSNVALQREEDRVEQKEAEVGELQRRLLG 238
Cdd:COG4913   242 EALEDAREQI-ELLEPIRELAERYAaarerlAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  239 METEHQALLAKVRE-GEVALEELRSNNADCQAERE----KAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 313
Cdd:COG4913   321 LREELDELEAQIRGnGGDRLEQLEREIERLERELEererRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                         170       180
                  ....*....|....*....|....*..
gi 119573814  314 AVIQSK----DATIQELKEKIAYLEAE 336
Cdd:COG4913   401 EALEEAlaeaEAALRDLRRELRELEAE 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
219-367 3.28e-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: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  219 EDRVEQKEAEVGELQRRLlgmeTEHQALLAKVREGEVALEELRSNNADCQA---EREKAATLEKEVAGLREKIHHLD--- 292
Cdd:COG4913   609 RAKLAALEAELAELEEEL----AEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDass 684
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119573814  293 DMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQARAKTEN 367
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
106-345 4.55e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 106 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 179
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 180 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 245
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 246 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 308
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119573814 309 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 345
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
180-345 5.20e-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: 42.35  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   180 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR-------E 252
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   253 GEVALEELRSNNADCQAE----REKAATLEKEVAGLREKI--------------HHLDDMLKSQQRKVRQMIEQLQNSKA 314
Cdd:TIGR02168  321 LEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELeeleaeleelesrlEELEEQLETLRSKVAQLELQIASLNN 400
                          170       180       190
                   ....*....|....*....|....*....|.
gi 119573814   315 VIQSKDATIQELKEKIAYLEAENLEMHDRME 345
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-335 5.29e-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: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  201 LSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG---------METEHQALLAKVREGEVALEELRSNNADCQAER 271
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSDDLAALE 691
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119573814  272 EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQElkEKIAYLEA 335
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEE 753
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
218-350 6.15e-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: 41.98  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  218 EEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDdmlkS 297
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ----S 377
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119573814  298 QQRKVRQMIEQLQNskAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEK 350
Cdd:pfam05622 378 ELQKKKEQIEELEP--KQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEK 428
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
167-352 7.23e-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: 41.29  E-value: 7.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 167 EDVESLRKTVQDLLAKLQEAKRQHQSdcvaFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET---EH 243
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 244 QALLAKV-----REGEVALEELRSNNADC--------------QAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQ 304
Cdd:COG4942  103 KEELAELlralyRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119573814 305 MIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH---DRMEHLIEKQI 352
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEALIARLE 233
DUF1068 pfam06364
Protein of unknown function (DUF1068); This family consists of several hypothetical plant ...
159-239 8.02e-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: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814  159 PEVdtciNEDVEslrKTVQDLLA---KLQEA---KRQHQSDCVAFEV--TLSRYQREAEQSNVALQREEDRVEQKEAEVG 230
Cdd:pfam06364  72 PEV----SEEME---KNFADLLSeelKLQEAvalENQHRADMALLEAkkIASQYQKEADKCNSGMETCEEAREKAEAALV 144

                  ....*....
gi 119573814  231 ElQRRLLGM 239
Cdd:pfam06364 145 E-QRKLTAL 152
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
214-336 1.10e-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: 40.29  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 214 ALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSN------NADCQAEREKAATLEKEVAGLREK 287
Cdd:COG1579   39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealQKEIESLKRRISDLEDEILELMER 118
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119573814 288 IHHLDDMLKSQQRKVRQMIEQLqnsKAVIQSKDATIQELKEKIAYLEAE 336
Cdd:COG1579  119 IEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-352 1.30e-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: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   201 LSRYQREAEQSNvalqreedRVEQKEAEVGELQRRLLGMEtehqaLLAKVREGEVALEELRSNNADCQAEREKAATLEKE 280
Cdd:TIGR02168  202 LKSLERQAEKAE--------RYKELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119573814   281 VAGLREKIHHLDDMLKSQQRKvrqmieqLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 352
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
167-336 2.08e-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: 39.75  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 167 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQ------------------KEAE 228
Cdd:COG4942   51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPED 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 229 VGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKihhLDDMLKSQQRKVRQMIEQ 308
Cdd:COG4942  131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKE 207
                        170       180
                 ....*....|....*....|....*...
gi 119573814 309 LQNSKAVIQSKDATIQELKEKIAYLEAE 336
Cdd:COG4942  208 LAELAAELAELQQEAEELEALIARLEAE 235
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
165-363 2.59e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 165 INEDVESLRKTVQDLLAKLQEAKRQHQSdcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRL-------- 236
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalp 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 237 -LGMETEHQALLAKVREGEVALEELRS----NNADCQAEREKAATLEK----EVAGLREKIHHLDDMLKSQQRKVRQMIE 307
Cdd:COG3206  258 eLLQSPVIQQLRAQLAELEAELAELSArytpNHPDVIALRAQIAALRAqlqqEAQRILASLEAELEALQAREASLQAQLA 337
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119573814 308 QLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHL-IEKQISHGNFSTQARA 363
Cdd:COG3206  338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEArLAEALTVGNVRVIDPA 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-313 2.93e-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: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814    96 INQLKSEVQYIQEARNCLQKLREDISSKLDRN------LGDSLHRQE--IQVVLEKPNGFSQSPTALYSSPPEVDTcINE 167
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEekLEELKEELESLEAELEELEAELEELES-RLE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814   168 DVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEqsNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 247
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119573814   248 AKVREGEVALEELRSNNADCQAEREKAatlEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 313
Cdd:TIGR02168  454 EELERLEEALEELREELEEAEQALDAA---ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
167-317 3.17e-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: 39.28  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 167 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 237
Cdd:cd22656  110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 238 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAAtlekevaglrekihHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 317
Cdd:cd22656  189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAAL--------------RLIADLTAADTDLDNLLALIGPAIPALE 249
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
167-336 4.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 167 EDVESLRKTVQDLLAKLQEAKRQHQSdcvafevtLSRYQREAEQSNVALQREEDRVEQKEA------EVGELQRRLLGME 240
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELP 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 241 TEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIhhlddmLKSQQRKVRQMIEQLQNSKAVIQSKD 320
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQ 219
                        170
                 ....*....|....*.
gi 119573814 321 ATIQELKEKIAYLEAE 336
Cdd:COG4717  220 EELEELEEELEQLENE 235
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
203-310 5.95e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 203 RYQREAEQSNVALQREEDRVEQKEAEVGELqrrllgmETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVA 282
Cdd:COG2433  396 EAEREKEHEERELTEEEEEIRRLEEQVERL-------EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS 468
                         90       100
                 ....*....|....*....|....*...
gi 119573814 283 GLREKIhhldDMLKSQQRKVRQMIEQLQ 310
Cdd:COG2433  469 RLDREI----ERLERELEEERERIEELK 492
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
205-296 7.05e-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: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 205 QREAEQSnvALQREEDRVEQKEAEvgELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGL 284
Cdd:COG0542  422 QLEIEKE--ALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497
                         90
                 ....*....|..
gi 119573814 285 REKIHHLDDMLK 296
Cdd:COG0542  498 EEELAELAPLLR 509
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
219-337 9.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 219 EDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQ 298
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119573814 299 QRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAEN 337
Cdd:PRK03918 272 KKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
PLN02939 PLN02939
transferase, transferring glycosyl groups
177-335 9.05e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 38.34  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 177 QDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALlakvregEVA 256
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLL-------DAS 272
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119573814 257 LEELRSNNADCQAEREKAATLEKEVagLREKIHHLDDMLKSQQRKVRQMIEQLQNSkaviqskdatiQELKEKIAYLEA 335
Cdd:PLN02939 273 LRELESKFIVAQEDVSKLSPLQYDC--WWEKVENLQDLLDRATNQVEKAALVLDQN-----------QDLRDKVDKLEA 338
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
256-356 9.96e-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: 37.82  E-value: 9.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119573814 256 ALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEA 335
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
                         90       100
                 ....*....|....*....|.
gi 119573814 336 ENLEMHDRMEHLIEKQISHGN 356
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGR 118
 
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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