NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462513301|ref|XP_054194564|]
View 

tuftelin isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2462513301 114 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 186
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 187 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 262
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462513301 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 2462513301 114 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 186
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 187 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 262
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462513301 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 2462513301  108 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  187 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 266
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          170
                   ....*....|....*
gi 2462513301  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 2462513301  111 ESLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQAL 187
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  188 LAKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNS 253
Cdd:pfam15921  534 QHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEF 609
                          170       180
                   ....*....|....*....|....*...
gi 2462513301  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 2462513301  47 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 120
Cdd:PRK02224  281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:PRK02224  358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 187 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 249
Cdd:PRK02224  438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462513301 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 2462513301 108 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 178
Cdd:cd22656   110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 179 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAATlekevagLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 258
Cdd:cd22656   189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAALR-------LIADLTAADTDLDNLLALIGPAIPALEKLQGAWQ 256
                         170
                  ....*....|...
gi 2462513301 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 2462513301 114 RKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 186
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 187 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 262
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462513301 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 2462513301 106 INEDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 182
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 183 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 261
Cdd:COG1196   331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                         170
                  ....*....|....*....
gi 2462513301 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 2462513301 162 RVEQ--KEAEVGELQRRLLGMETEHQALlakVREGEvaleelrsnnadcQAEREKAATLEKEVAGLREKIhhldDMLKSQ 239
Cdd:COG0542   403 RMEIdsKPEELDELERRLEQLEIEKEAL---KKEQD-------------EASFERLAELRDELAELEEEL----EALKAR 462
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462513301 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 2462513301  108 EDVESLRKTVQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  187 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 266
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          170
                   ....*....|....*
gi 2462513301  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 2462513301 146 QREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKaatLEKEVAGL 225
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARL 300
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513301 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 2462513301  111 ESLRKtVQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQAL 187
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  188 LAKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNS 253
Cdd:pfam15921  534 QHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEF 609
                          170       180
                   ....*....|....*....|....*...
gi 2462513301  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 2462513301  165 QKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREkaaTLEKEVAGLREKIHHLDDMLKSQQRKVR 244
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462513301  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 2462513301   34 EKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNLGD-SLHRQEIQVVLEKPNGFSQSPTALYSSPPEVDTCINEdVES 112
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  113 LRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG------------- 179
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqieelsedie 855
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  180 ---------------METEHQALLAKVREGEVALEELRSnnaDCQAEREKAATLEKEVAGLREKIHHLddmlksqqrkvR 244
Cdd:TIGR02168  856 slaaeieeleelieeLESELEALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEEL-----------R 921
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462513301  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 2462513301   37 INQLKSEVQYIQEARNCLQKLREDISSKLDR-------------NLGDSLHRQEIQVVLEKPNGFSQSPTALYSSPPEVD 103
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEEleedlhkleealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  104 TCINE---DVESLRKTVQDLLAKLQEAKRQHQSDCvafevtlsryqREAEQSNVALQREEDRVEQKEAEVGELQRRLLGM 180
Cdd:TIGR02169  819 QKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIE-----------KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  181 ETEHQALLAKVREGEVALEELrsnNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQ---------RKVRQMIEQLQ 251
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEEL---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVE 964
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462513301  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 2462513301  109 DVESLRKTVQDLLAKLQEAKrqhqsdcvAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 188
Cdd:COG4913    662 DVASAEREIAELEAELERLD--------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  189 AKVREGEVA--------LEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLksqqrkVRQMIEQLQNSKAVIQSK 260
Cdd:COG4913    734 DRLEAAEDLarlelralLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADL 807
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462513301  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 2462513301 156 LQREEDRVEQKEAEVGELQR-----------RLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKA----ATLEK 220
Cdd:COG1196   188 LERLEDILGELERQLEPLERqaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELeaelAELEA 267
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462513301 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 2462513301   33 HEKNINQLKSEVQYIQEARNCLQKLREDISSKLdRNLGDSLHRQEIQVVLEKpngfsqsptalyssppevdtcinEDVES 112
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSRQISALR-----------------------KDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  113 LRKTVQdllaKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 192
Cdd:TIGR02168  738 LEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  193 EGEVALEELRSNNADCQAEREKAAT----LEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQ---NSKAVIQ------- 258
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERrledLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEealallr 893
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462513301  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 2462513301 121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEE 200
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 201 LRSNNADcqAEREKA------ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYL 274
Cdd:COG1196   405 LEEAEEA--LLERLErleeelEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462513301 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 2462513301  108 EDVESLRKTVqDLLAKLQEAKRQHQ------SDCVAFEVTLSRY--QREAEQSNVALQREEDRVEQKEAEVGELQRRLLG 179
Cdd:COG4913    242 EALEDAREQI-ELLEPIRELAERYAaarerlAELEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  180 METEHQALLAKVRE-GEVALEELRSNNADCQAERE----KAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSK 254
Cdd:COG4913    321 LREELDELEAQIRGnGGDRLEQLEREIERLERELEererRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
                          170       180
                   ....*....|....*....|....*..
gi 2462513301  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 2462513301  160 EDRVEQKEAEVGELQRRLlgmeTEHQALLAKVREGEVALEELRSNNADCQA---EREKAATLEKEVAGLREKIHHLD--- 233
Cdd:COG4913    609 RAKLAALEAELAELEEEL----AEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDass 684
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462513301  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 2462513301  142 LSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG---------METEHQALLAKVREGEVALEELRSNNADCQAER 212
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSDDLAALE 691
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462513301  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 2462513301  47 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTVQDL--- 120
Cdd:PRK02224  281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 186
Cdd:PRK02224  358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 187 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 249
Cdd:PRK02224  438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2462513301 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 2462513301  121 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR-------E 193
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleE 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  194 GEVALEELRSNNADCQAE----REKAATLEKEVAGLREKI--------------HHLDDMLKSQQRKVRQMIEQLQNSKA 255
Cdd:TIGR02168  321 LEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELeeleaeleelesrlEELEEQLETLRSKVAQLELQIASLNN 400
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462513301  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 2462513301 100 PEVdtciNEDVEslrKTVQDLLA---KLQEA---KRQHQSDCVAFEV--TLSRYQREAEQSNVALQREEDRVEQKEAEVG 171
Cdd:pfam06364  72 PEV----SEEME---KNFADLLSeelKLQEAvalENQHRADMALLEAkkIASQYQKEADKCNSGMETCEEAREKAEAALV 144

                  ....*....
gi 2462513301 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 2462513301 159 EEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDdmlkS 238
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ----S 377
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462513301 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 2462513301 108 EDVESLRKTVQDLLAKLQEAKRQHQSdcvaFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET---EH 184
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 185 QALLAKV-----REGEVALEELRSNNADC--------------QAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQ 245
Cdd:COG4942   103 KEELAELlralyRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462513301 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 2462513301  142 LSRYQREAEQSNvalqreedRVEQKEAEVGELQRRLLGMEtehqaLLAKVREGEVALEELRSNNADCQAEREKAATLEKE 221
Cdd:TIGR02168  202 LKSLERQAEKAE--------RYKELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEK 268
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462513301  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 2462513301 155 ALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSN------NADCQAEREKAATLEKEVAGLREK 228
Cdd:COG1579    39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealQKEIESLKRRISDLEDEILELMER 118
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462513301 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 2462513301 108 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQ------------------KEAE 169
Cdd:COG4942    51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPED 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 170 VGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKihhLDDMLKSQQRKVRQMIEQ 249
Cdd:COG4942   131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKE 207
                         170       180
                  ....*....|....*....|....*...
gi 2462513301 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 2462513301 106 INEDVESLRKTVQDLLAKLQEAKRQHQSdcVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRL-------- 177
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalp 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 178 -LGMETEHQALLAKVREGEVALEELRS----NNADCQAEREKAATLEK----EVAGLREKIHHLDDMLKSQQRKVRQMIE 248
Cdd:COG3206   258 eLLQSPVIQQLRAQLAELEAELAELSArytpNHPDVIALRAQIAALRAqlqqEAQRILASLEAELEALQAREASLQAQLA 337
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513301 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 2462513301 108 EDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK---------EAEVGELQRRLl 178
Cdd:cd22656   110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltdeggaiaRKEIKDLQKEL- 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 179 gmETEHQALLAKVREgevALEELRSNNADCQAEREKAATlekevagLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQ 258
Cdd:cd22656   189 --EKLNEEYAAKLKA---KIDELKALIADDEAKLAAALR-------LIADLTAADTDLDNLLALIGPAIPALEKLQGAWQ 256
                         170
                  ....*....|...
gi 2462513301 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 2462513301   37 INQLKSEVQYIQEARNCLQKLREDISSKLDRN------LGDSLHRQE--IQVVLEKPNGFSQSPTALYSSPPEVDTcINE 108
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELeskldeLAEELAELEekLEELKEELESLEAELEELEAELEELES-RLE 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  109 DVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEqsNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 188
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462513301  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 2462513301 144 RYQREAEQSNVALQREEDRVEQKEAEVGELqrrllgmETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVA 223
Cdd:COG2433   396 EAEREKEHEERELTEEEEEIRRLEEQVERL-------EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS 468
                          90       100
                  ....*....|....*....|....*...
gi 2462513301 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 2462513301 146 QREAEQSnvALQREEDRVEQKEAEvgELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGL 225
Cdd:COG0542   422 QLEIEKE--ALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497
                          90
                  ....*....|..
gi 2462513301 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 2462513301  110 VESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTL------------SRYQREAEQSNV--ALQREEDRVEQKEAEVG---E 172
Cdd:pfam15921  319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselteartERDQFSQESGNLddQLQKLLADLHKREKELSlekE 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301  173 LQRRLLGMETEHQALLAKVREG------EVALEE--LRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVR 244
Cdd:pfam15921  399 QNKRLWDRDTGNSITIDHLRRElddrnmEVQRLEalLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLR 478
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2462513301  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 2462513301 108 EDVESLRKTVQDLLAKLQEAKRQHQSdcvafevtLSRYQREAEQSNVALQREEDRVEQKEA------EVGELQRRLLGME 181
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513301 182 TEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIhhlddmLKSQQRKVRQMIEQLQNSKAVIQSKD 261
Cdd:COG4717   146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQ 219
                         170
                  ....*....|....*.
gi 2462513301 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 2462513301 118 QDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALlakvregEVA 197
Cdd:PLN02939  200 EEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLL-------DAS 272
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513301 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure