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Conserved domains on  [gi|221042994|dbj|BAH13174|]
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unnamed protein product [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]; ...
 113-287 3.95e-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: 51.86  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 113 INEDVESLRKTMQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 189
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 190 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 268
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        170
                 ....*....|....*....
gi 221042994 269 ATIQELKEKIAYLEAENLE 287
Cdd:COG1196  411 ALLERLERLEEELEELEEA 429
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-287 3.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 113 INEDVESLRKTMQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 189
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 190 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 268
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        170
                 ....*....|....*....
gi 221042994 269 ATIQELKEKIAYLEAENLE 287
Cdd:COG1196  411 ALLERLERLEEELEELEEA 429
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-288 9.76e-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: 47.37  E-value: 9.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   115 EDVESLRKTMQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 193
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   194 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 273
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928

                          170
                   ....*....|....*
gi 221042994   274 LKEKIAYLEAENLEM 288
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 118-288 3.44e-05

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: 45.88  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   118 ESLRKtMQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQAL 194
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   195 LAKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNS 260
Cdd:pfam15921  534 QHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEF 609

                          170       180
                   ....*....|....*....|....*...
gi 221042994   261 KAVIQSKDATIQELKEKIAYLEAENLEM 288
Cdd:pfam15921  610 KILKDKKDAKIRELEARVSDLELEKVKL 637
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
54-293 1.94e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  54 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTMQDL--- 127
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 128 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 193
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 194 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 256
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 221042994 257 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 293
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-287 3.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 113 INEDVESLRKTMQDLLAKLQEAKRQHQSDCVAFEVTLSRYQ---REAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET 189
Cdd:COG1196  251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEE 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 190 EHQALLAKVREGEVALEELRSNNADCQAER-EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 268
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        170
                 ....*....|....*....
gi 221042994 269 ATIQELKEKIAYLEAENLE 287
Cdd:COG1196  411 ALLERLERLEEELEELEEA 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 121-301 5.48e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 121 RKTMQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQK-------EAEVGELQRRLLGMETEHQA 193
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 194 LLAKVREGEVALEELRSNNADCQAEREKA----ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDA 269
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELeeelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190
                 ....*....|....*....|....*....|..
gi 221042994 270 TIQELKEKIAYLEAENLEMHDRMEHLIEKQIS 301
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEE 425
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 169-289 7.17e-07

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 50.85  E-value: 7.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 169 RVEQ--KEAEVGELQRRLLGMETEHQALlakVREGEvaleelrsnnadcQAEREKAATLEKEVAGLREKIhhldDMLKSQ 246
Cdd:COG0542  403 RMEIdsKPEELDELERRLEQLEIEKEAL---KKEQD-------------EASFERLAELRDELAELEEEL----EALKAR 462

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 221042994 247 QRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH 289
Cdd:COG0542  463 WEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELA 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-299 5.96e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 5.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 116 DVESLRKTMQDLLAKLQEAKRQHQsdcvAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 195
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELE----ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 196 AKVREGEVALEELRSNNADCQAER----EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATI 271
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELaeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                        170       180
                 ....*....|....*....|....*...
gi 221042994 272 QELKEKIAYLEAENLEMHDRMEHLIEKQ 299
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAE 409
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 115-288 9.76e-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: 47.37  E-value: 9.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   115 EDVESLRKTMQDLLAKLQEAK-RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 193
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   194 LLAKVREGEVALEELRSNNADCQAErekAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQE 273
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928

                          170
                   ....*....|....*
gi 221042994   274 LKEKIAYLEAENLEM 288
Cdd:TIGR02169  929 LEEELSEIEDPKGED 943
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 172-299 1.22e-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: 46.98  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   172 QKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREkaaTLEKEVAGLREKIHHLDDMLKSQQRKVR 251
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 221042994   252 QMIEQLQNSKAVIQSKDATIQELKEKIAYLEAE--NLEMHDRMEHLIEKQ 299
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLSHSRIPEIQ 797
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-299 1.71e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 120 LRKTMQDLLAKLQEAKRQHqsdcvaFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 199
Cdd:COG1196  218 LKEELKELEAELLLLKLRE------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 200 EGEVALEELRsnnADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIA 279
Cdd:COG1196  292 ELLAELARLE---QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                        170       180
                 ....*....|....*....|
gi 221042994 280 YLEAENLEMHDRMEHLIEKQ 299
Cdd:COG1196  369 EAEAELAEAEEELEELAEEL 388
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 118-288 3.44e-05

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: 45.88  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   118 ESLRKtMQDLLAKLQEAK---RQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLlgmETEHQAL 194
Cdd:pfam15921  458 ESLEK-VSSLTAQLESTKemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV---DLKLQEL 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   195 LAKVREGEvaleELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIE--------------QLQNS 260
Cdd:pfam15921  534 QHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVekaqlekeindrrlELQEF 609

                          170       180
                   ....*....|....*....|....*...
gi 221042994   261 KAVIQSKDATIQELKEKIAYLEAENLEM 288
Cdd:pfam15921  610 KILKDKKDAKIRELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 44-298 4.49e-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: 45.44  E-value: 4.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994    44 INQLKSEVQYIQEARNCLQKLREDISSKLDR-------------NLGDSLHRQEIQVVLEKPNGFSQSPTALYSSPPEVD 110
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEEleedlhkleealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   111 TCINE---DVESLRKTMQDLLAKLQEAKRQHQSDCvafevtlsryqREAEQSNVALQREEDRVEQKEAEVGELQRRLLGM 187
Cdd:TIGR02169  819 QKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIE-----------KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   188 ETEHQALLAKVREGEVALEELrsnNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQ---------RKVRQMIEQLQ 258
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEEL---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelslEDVQAELQRVE 964

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 221042994   259 ---------NSKAVIQSKD--ATIQELKEKIAYLEAENLEMHDRMEHLIEK 298
Cdd:TIGR02169  965 eeiralepvNMLAIQEYEEvlKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 36-301 5.35e-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: 45.05  E-value: 5.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994    36 DKMIHEKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNlgdSLHRQEIQVVLEKPNgfsqsptalysspPEVDTcINE 115
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA---EEELAEAEAEIEELE-------------AQIEQ-LKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   116 DVESLRKTMQDLLAKLQEAKR---QHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQ 192
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   193 ALLAKVREGEVALEELRSnnaDCQAEREKAATLEKEVAGLREKIHHLddmlksqqrkvRQMIEQLQNSKAVIQskdATIQ 272
Cdd:TIGR02168  877 ALLNERASLEEALALLRS---ELEELSEELRELESKRSELRRELEEL-----------REKLAQLELRLEGLE---VRID 939

                          250       260
                   ....*....|....*....|....*....
gi 221042994   273 ELKEKIAYLEAENLEMHDRMEHLIEKQIS 301
Cdd:TIGR02168  940 NLQERLSEEYSLTLEEAEALENKIEDDEE 968
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
116-311 8.87e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 8.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  116 DVESLRKTMQDLLAKLQEAKrqhqsdcvAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALL 195
Cdd:COG4913   662 DVASAEREIAELEAELERLD--------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  196 AKVREGEVA--------LEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLksqqrkVRQMIEQLQNSKAVIQSK 267
Cdd:COG4913   734 DRLEAAEDLarlelralLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADL 807

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 221042994  268 DATIQELKEKIAY---LEAENLEMH-DRMEHLIEKQISH--GNFSTQARA 311
Cdd:COG4913   808 DADLESLPEYLALldrLEEDGLPEYeERFKELLNENSIEfvADLLSKLRR 857
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-300 1.00e-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: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 163 LQREEDRVEQKEAEVGELQR-----------RLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKA----ATLEK 227
Cdd:COG1196  188 LERLEDILGELERQLEPLERqaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELeaelAELEA 267

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221042994 228 EVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 300
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 156-299 1.31e-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: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 156 AEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAE----REKAATLEKEVAG 231
Cdd:COG1196  206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEleelRLELEELELELEE 285

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221042994 232 LREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 299
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 115-321 1.85e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 115 EDVESLRKTMQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQAL 194
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 195 LAKVREGEVALEELRSNNADcqAEREKA------ATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKD 268
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEA--LLERLErleeelEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 221042994 269 ATIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQARAKTENPGSIRI 321
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
153-284 3.75e-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: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  153 QREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVRE-GEVALEELRSNNADCQAERE----KAATLEK 227
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEererRRARLEA 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221042994  228 EVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSK----DATIQELKEKIAYLEAE 284
Cdd:COG4913   367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAE 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
167-315 4.02e-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: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  167 EDRVEQKEAEVGELQRRLlgmeTEHQALLAKVREGEVALEELRSNNADCQA---EREKAATLEKEVAGLREKIHHLD--- 240
Cdd:COG4913   609 RAKLAALEAELAELEEEL----AEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAELEAELERLDass 684

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042994  241 DMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQARAKTEN 315
Cdd:COG4913   685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-299 4.24e-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: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994    40 HEKNINQLKSEVQYIQEARNCLQKLREDISSKLdRNLGDSLHRQEIQVVLEKpngfsqsptalyssppevdtcinEDVES 119
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSRQISALR-----------------------KDLAR 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   120 LRKTMQdllaKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR 199
Cdd:TIGR02168  738 LEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   200 EGEVALEELRSNNADCQAEREKAAT----LEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQ---NSKAVIQ------- 265
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERrledLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEealallr 893

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 221042994   266 ----SKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQ 299
Cdd:TIGR02168  894 seleELSEELRELESKRSELRRELEELREKLAQLELRL 931
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
149-283 6.06e-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: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  149 LSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLG---------METEHQALLAKVREGEVALEELRSNNADCQAER 219
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSDDLAALE 691

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221042994  220 EKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQElkEKIAYLEA 283
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEE 753
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-300 7.06e-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: 40.90  E-value: 7.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 115 EDVESLRKTMQDLLAKLQEAKRQHQSdcvaFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMET---EH 191
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 192 QALLAKV-----REGEVALEELRSNNADC--------------QAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQ 252
Cdd:COG4942  103 KEELAELlralyRLGRQPPLALLLSPEDFldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221042994 253 MIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMH---DRMEHLIEKQI 300
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEALIARLE 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-293 1.31e-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: 40.81  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   128 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVR-------E 200
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqleE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   201 GEVALEELRSNNADCQAE----REKAATLEKEVAGLREKI--------------HHLDDMLKSQQRKVRQMIEQLQNSKA 262
Cdd:TIGR02168  321 LEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELeeleaeleelesrlEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190
                   ....*....|....*....|....*....|.
gi 221042994   263 VIQSKDATIQELKEKIAYLEAENLEMHDRME 293
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLE 431
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 166-298 1.37e-03

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: 40.44  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  166 EEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDdmlkS 245
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQ----S 377

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 221042994  246 QQRKVRQMIEQLQNskAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEK 298
Cdd:pfam05622 378 ELQKKKEQIEELEP--KQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEK 428
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
54-293 1.94e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  54 IQEARNCLQKLREDISSKLDRNLGDSLhrqEIQVVLEKPNGFSQSPTALYSSPPEVDTCI---NEDVESLRKTMQDL--- 127
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDA---DAEAVEARREELEDRDEELRDRLEECRVAAqahNEEAESLREDADDLeer 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 128 LAKLQEAKRQHQSDCVAFEVTLSRYQREAEQ--------------SNVALQREEDRVEQKEAEVGELQRRLLGMETEHQA 193
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRT 437

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 194 LLAKVREGEVALEELR----------SNNADCQAE-REKAATLEKEVAGLREKIHHLDDM------LKSQQRKVRQMIEQ 256
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEER 517

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 221042994 257 LQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRME 293
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
DUF1068 pfam06364
Protein of unknown function (DUF1068); This family consists of several hypothetical plant ...
 107-187 2.10e-03

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


Pssm-ID: 399393 [Multi-domain]  Cd Length: 165  Bit Score: 38.47  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994  107 PEVdtciNEDVEslrKTMQDLLA---KLQEA---KRQHQSDCVAFEV--TLSRYQREAEQSNVALQREEDRVEQKEAEVG 178
Cdd:pfam06364  72 PEV----SEEME---KNFADLLSeelKLQEAvalENQHRADMALLEAkkIASQYQKEADKCNSGMETCEEAREKAEAALV 144


                  ....*....
gi 221042994  179 ElQRRLLGM 187
Cdd:pfam06364 145 E-QRKLTAL 152
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 162-284 2.92e-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: 38.75  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 162 ALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSN------NADCQAEREKAATLEKEVAGLREK 235
Cdd:COG1579   39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealQKEIESLKRRISDLEDEILELMER 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 221042994 236 IHHLDDMLKSQQRKVRQMIEQLqnsKAVIQSKDATIQELKEKIAYLEAE 284
Cdd:COG1579  119 IEELEEELAELEAELAELEAEL---EEKKAELDEELAELEAELEELEAE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-300 3.07e-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: 39.65  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994   149 LSRYQREAEQSNvalqreedRVEQKEAEVGELQRRLLGMEtehqaLLAKVREGEVALEELRSNNADCQAEREKAATLEKE 228
Cdd:TIGR02168  202 LKSLERQAEKAE--------RYKELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221042994   229 VAGLREKIHHLDDMLKSQQRKvrqmieqLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQI 300
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-284 4.30e-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: 38.59  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 115 EDVESLRKTMQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQ------------------KEAE 176
Cdd:COG4942   51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPED 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 177 VGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKihhLDDMLKSQQRKVRQMIEQ 256
Cdd:COG4942  131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLARLEKE 207

                        170       180
                 ....*....|....*....|....*...
gi 221042994 257 LQNSKAVIQSKDATIQELKEKIAYLEAE 284
Cdd:COG4942  208 LAELAAELAELQQEAEELEALIARLEAE 235
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 153-244 6.58e-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: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 153 QREAEQSnvALQREEDRVEQKEAEvgELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGL 232
Cdd:COG0542  422 QLEIEKE--ALKKEQDEASFERLA--ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAEL 497

                         90
                 ....*....|..
gi 221042994 233 REKIHHLDDMLK 244
Cdd:COG0542  498 EEELAELAPLLR 509
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
151-258 7.55e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.92  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 151 RYQREAEQSNVALQREEDRVEQKEAEVGELqrrllgmETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVA 230
Cdd:COG2433  396 EAEREKEHEERELTEEEEEIRRLEEQVERL-------EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS 468

                         90       100
                 ....*....|....*....|....*...
gi 221042994 231 GLREKIhhldDMLKSQQRKVRQMIEQLQ 258
Cdd:COG2433  469 RLDREI----ERLERELEEERERIEELK 492
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
115-284 9.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 115 EDVESLRKTMQDLLAKLQEAKRQHQSdcvafevtLSRYQREAEQSNVALQREEDRVEQKEA------EVGELQRRLLGME 188
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEKLLQllplyqELEALEAELAELP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042994 189 TEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIhhlddmLKSQQRKVRQMIEQLQNSKAVIQSKD 268
Cdd:COG4717  146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQ 219

                        170
                 ....*....|....*.
gi 221042994 269 ATIQELKEKIAYLEAE 284
Cdd:COG4717  220 EELEELEEELEQLENE 235
 
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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