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Conserved domains on  [gi|2462603114|ref|XP_054208850|]
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protein Spindly isoform X3 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-282 4.50e-09

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   13 KQQQKMHLEKLEEQLSRShGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDH-QKELLSCKSE------ELRVMSERvQ 85
Cdd:TIGR02168  234 LEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEisrleqQKQILRER-L 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   86 ESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKeekeerekeavsyyNALEKARVANQDL 165
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------------AELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  166 QVQLDQAlqqaldpnskgNSLFAEVEDRRAAMERQLISMKVKYQSLKKqNVFNREQMQRMKLQIATLLQMKGSQTEFEQQ 245
Cdd:TIGR02168  378 EEQLETL-----------RSKVAQLELQIASLNNEIERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462603114  246 ERLLAMLEQKNGEIKHLLGEIRN-LEKFKNLYDSMESK 282
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREeLEEAEQALDAAERE 483
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-282 4.50e-09

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: 59.30  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   13 KQQQKMHLEKLEEQLSRShGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDH-QKELLSCKSE------ELRVMSERvQ 85
Cdd:TIGR02168  234 LEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEisrleqQKQILRER-L 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   86 ESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKeekeerekeavsyyNALEKARVANQDL 165
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------------AELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  166 QVQLDQAlqqaldpnskgNSLFAEVEDRRAAMERQLISMKVKYQSLKKqNVFNREQMQRMKLQIATLLQMKGSQTEFEQQ 245
Cdd:TIGR02168  378 EEQLETL-----------RSKVAQLELQIASLNNEIERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462603114  246 ERLLAMLEQKNGEIKHLLGEIRN-LEKFKNLYDSMESK 282
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREeLEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 14-214 8.07e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  14 QQQKMHLEKLEEQLSRSHGQ---EVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLScKSEELRVMSERVQESMSS 90
Cdd:COG1196   301 EQDIARLEERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  91 EMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVsyynALEKARVANQDLQVQLD 170
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----EEEEALEEAAEEEAELE 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462603114 171 QALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQ 214
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 10-368 3.68e-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: 46.65  E-value: 3.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   10 EAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSckseelrvmservQESMS 89
Cdd:pfam15921  518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG-------------QHGRT 584

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   90 SEmlALQIEltemesmKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQL 169
Cdd:pfam15921  585 AG--AMQVE-------KAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER 655

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  170 DQALQQALDPNSKGNSLFAEvedrraamerqlismkvkYQSLKKQNVFNREQMQRMKLQIAtlLQMKGSQTEFEQQERLL 249
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSED------------------YEVLKRNFRNKSEEMETTTNKLK--MQLKSAQSELEQTRNTL 715

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  250 AMLEQKNGE-IKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIEST-------KGELSIQ 321
Cdd:pfam15921  716 KSMEGSDGHaMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVateknkmAGELEVL 795

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2462603114  322 RMKALFESQRALDIERKLfaNERCLQLSESENMKLRAKLDELKLKYE 368
Cdd:pfam15921  796 RSQERRLKEKVANMEVAL--DKASLQFAECQDIIQRQEQESVRLKLQ 840
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-198 2.00e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   8 ECEAIKQQQKMHLEKLEEQLSRSHG--QEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ 85
Cdd:PRK02224  224 RYEEQREQARETRDEADEVLEEHEErrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  86 -ESMSSEMLALQIEltEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQD 164
Cdd:PRK02224  304 lDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED 381

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462603114 165 LQVQLDqALQQALDPNSK--GNS--LFAEVEDRRAAME 198
Cdd:PRK02224  382 RREEIE-ELEEEIEELRErfGDApvDLGNAEDFLEELR 418
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-282 4.50e-09

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: 59.30  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   13 KQQQKMHLEKLEEQLSRShGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDH-QKELLSCKSE------ELRVMSERvQ 85
Cdd:TIGR02168  234 LEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEisrleqQKQILRER-L 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   86 ESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKeekeerekeavsyyNALEKARVANQDL 165
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------------AELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  166 QVQLDQAlqqaldpnskgNSLFAEVEDRRAAMERQLISMKVKYQSLKKqNVFNREQMQRMKLQIATLLQMKGSQTEFEQQ 245
Cdd:TIGR02168  378 EEQLETL-----------RSKVAQLELQIASLNNEIERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462603114  246 ERLLAMLEQKNGEIKHLLGEIRN-LEKFKNLYDSMESK 282
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREeLEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 14-214 8.07e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  14 QQQKMHLEKLEEQLSRSHGQ---EVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLScKSEELRVMSERVQESMSS 90
Cdd:COG1196   301 EQDIARLEERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  91 EMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVsyynALEKARVANQDLQVQLD 170
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----EEEEALEEAAEEEAELE 455

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462603114 171 QALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQ 214
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-271 2.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   2 LESLSCECEAIKQQQKmHLEKLEEQLSrshgQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLscksEELRVMS 81
Cdd:COG1196   248 LEELEAELEELEAELA-ELEAELEELR----LELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEERL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  82 ERVQEsmssEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVA 161
Cdd:COG1196   319 EELEE----ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114 162 NQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQnvfNREQMQRMKLQIATLLQMKGSQTE 241
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA---AEEEAELEEEEEALLELLAELLEE 471

                         250       260       270
                  ....*....|....*....|....*....|
gi 2462603114 242 FEQQERLLAMLEQKNGEIKHLLGEIRNLEK 271
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLLEAEA 501
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
8-137 3.53e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114    8 ECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ-- 85
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAal 392

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462603114   86 -ESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRL 137
Cdd:COG4913    393 lEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 10-368 3.68e-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: 46.65  E-value: 3.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   10 EAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSckseelrvmservQESMS 89
Cdd:pfam15921  518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG-------------QHGRT 584

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   90 SEmlALQIEltemesmKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQL 169
Cdd:pfam15921  585 AG--AMQVE-------KAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQER 655

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  170 DQALQQALDPNSKGNSLFAEvedrraamerqlismkvkYQSLKKQNVFNREQMQRMKLQIAtlLQMKGSQTEFEQQERLL 249
Cdd:pfam15921  656 DQLLNEVKTSRNELNSLSED------------------YEVLKRNFRNKSEEMETTTNKLK--MQLKSAQSELEQTRNTL 715

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  250 AMLEQKNGE-IKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIEST-------KGELSIQ 321
Cdd:pfam15921  716 KSMEGSDGHaMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVateknkmAGELEVL 795

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2462603114  322 RMKALFESQRALDIERKLfaNERCLQLSESENMKLRAKLDELKLKYE 368
Cdd:pfam15921  796 RSQERRLKEKVANMEVAL--DKASLQFAECQDIIQRQEQESVRLKLQ 840
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-320 6.33e-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: 6.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114    2 LESLSCECEAIKQQQKMHLEKLEEQLSrSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMS 81
Cdd:TIGR02169  200 LERLRREREKAERYQALLKEKREYEGY-ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   82 ERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVA 161
Cdd:TIGR02169  279 KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  162 NQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAME---RQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLlqmKGS 238
Cdd:TIGR02169  359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGI---EAK 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  239 QTEFEqqerllAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKpsvdsgtledntyytdlLQMKLDNLNKEIESTKGEL 318
Cdd:TIGR02169  436 INELE------EEKEDKALEIKKQEWKLEQLAADLSKYEQELYD-----------------LKEEYDRVEKELSKLQREL 492


                   ..
gi 2462603114  319 SI 320
Cdd:TIGR02169  493 AE 494
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-236 2.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   20 LEKLEEQlsRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQK-ELLSCKSEELRVMSERVQEsmssEMLALQIE 98
Cdd:COG4913    244 LEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEA----ELERLEAR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   99 LTEMESMKTTLKEEVNELQYRQ-EQLELLITNLMRQVDRLKEEKEEREKEAvsyyNALEKARVANQD----LQVQLDQAL 173
Cdd:COG4913    318 LDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALL----AALGLPLPASAEefaaLRAEAAALL 393

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462603114  174 QQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMK 236
Cdd:COG4913    394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
25-278 2.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   25 EQLSRSHgQEVNELKTKIEKLKvELDEARLSEKQLKHQVDHQKELLscksEELRVmsERVQEsmssEMLALQIELTEMES 104
Cdd:COG4913    235 DDLERAH-EALEDAREQIELLE-PIRELAERYAAARERLAELEYLR----AALRL--WFAQR----RLELLEAELEELRA 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  105 MKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKeekeerekeavsyYNALEkarvanqDLQVQLDQALQQAldpnskgn 184
Cdd:COG4913    303 ELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLE-------QLEREIERLEREL-------- 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  185 slfAEVEDRRAAMERQLismkvkyQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTE--FEQQERLLAMLEQKNGEIKHL 262
Cdd:COG4913    355 ---EERERRRARLEALL-------AALGLPLPASAEEFAALRAEAAALLEALEEELEalEEALAEAEAALRDLRRELREL 424

                          250
                   ....*....|....*.
gi 2462603114  263 LGEIRNLEKFKNLYDS 278
Cdd:COG4913    425 EAEIASLERRKSNIPA 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-271 3.03e-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: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  19 HLEKLEEQLSRSHgQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQEsmssemlaLQIE 98
Cdd:COG1196   233 KLRELEAELEELE-AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR--------LEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  99 LTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAvsyyNALEKARVANQDLQVQLDQALQQALD 178
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL----EEAEAELAEAEEALLEAEAELAEAEE 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114 179 pnskgnsLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQmkgsqtEFEQQERLLAMLEQKNGE 258
Cdd:COG1196   380 -------ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE------ALAELEEEEEEEEEALEE 446

                         250
                  ....*....|...
gi 2462603114 259 IKHLLGEIRNLEK 271
Cdd:COG1196   447 AAEEEAELEEEEE 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 8-268 4.65e-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: 43.12  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114    8 ECEAIKQQQKMHLEKLE--EQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ 85
Cdd:TIGR02168  692 KIAELEKALAELRKELEelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   86 ES--------------------MSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKE----EK 141
Cdd:TIGR02168  772 EAeeelaeaeaeieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqieeLS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  142 EEREKEAVS------YYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLismkvkyQSLKKQN 215
Cdd:TIGR02168  852 EDIESLAAEieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKL 924

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462603114  216 VFNREQMQRMKLQIATLLQM--KGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRN 268
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-197 5.35e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  20 LEKLEEQLSRSHgQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLScksEELRVM------------------- 80
Cdd:COG4942    57 LAALERRIAALA-RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALyrlgrqpplalllspedfl 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  81 -SERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKeavsyynALEKAR 159
Cdd:COG4942   133 dAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK-------LLARLE 205

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462603114 160 VANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAM 197
Cdd:COG4942   206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 14-203 8.10e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  14 QQQKMHLEKLEEQLSRSHgQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELR--------------- 78
Cdd:COG3883    26 SELQAELEAAQAELDALQ-AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsggsvsy 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  79 -----------------VMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDrlkeek 141
Cdd:COG3883   105 ldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA------ 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462603114 142 eerekEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLIS 203
Cdd:COG3883   179 -----EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-196 1.32e-03

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: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   20 LEKLEEQLSRShGQEVNELKTKIEKLKVELD---EARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ-ESMSSEMLAL 95
Cdd:COG4913    612 LAALEAELAEL-EEELAEAEERLEALEAELDalqERREALQRLAEYSWDEIDVASAEREIAELEAELERlDASSDDLAAL 690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   96 QIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVAN-------QDLQVQ 168
Cdd:COG4913    691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgdaveRELREN 770

                          170       180
                   ....*....|....*....|....*...
gi 2462603114  169 LDQALQQAldpNSKGNSLFAEVEDRRAA 196
Cdd:COG4913    771 LEERIDAL---RARLNRAEEELERAMRA 795
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-198 2.00e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   8 ECEAIKQQQKMHLEKLEEQLSRSHG--QEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ 85
Cdd:PRK02224  224 RYEEQREQARETRDEADEVLEEHEErrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  86 -ESMSSEMLALQIEltEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQD 164
Cdd:PRK02224  304 lDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED 381

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462603114 165 LQVQLDqALQQALDPNSK--GNS--LFAEVEDRRAAME 198
Cdd:PRK02224  382 RREEIE-ELEEEIEELRErfGDApvDLGNAEDFLEELR 418
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 20-142 2.09e-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: 39.91  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  20 LEKLEEQLSRsHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEEL-RVMSERvqesmssEMLALQIE 98
Cdd:COG1579    26 LKELPAELAE-LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNK-------EYEALQKE 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462603114  99 LTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKE 142
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE 141
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 35-368 2.44e-03

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: 40.82  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   35 VNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEElRVMSERVQesmssemlALQIELTEMEsmkttLKEEVN 114
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQ--------ALLKEKREYE-----GYELLK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  115 ELQYRQEQLEllitNLMRQVDRLKEEkeerekeavsyynaLEKARVANQDLQVQLDQALQQALDPNSKgnsLFAEVEDRR 194
Cdd:TIGR02169  231 EKEALERQKE----AIERQLASLEEE--------------LEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQ 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  195 AAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEfeQQERLLAMLEQKNGEIKHLLGEIRNLEKFKN 274
Cdd:TIGR02169  290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA--EIEELEREIEEERKRRDKLTEEYAELKEELE 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  275 LYDSMESKPSVDSGTLEDNTyytDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENM 354
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDEL---KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444

                          330
                   ....*....|....
gi 2462603114  355 KLRAKLDELKLKYE 368
Cdd:TIGR02169  445 DKALEIKKQEWKLE 458
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 41-232 3.29e-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: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  41 KIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESmSSEMLALQIELTEMESMKTTLKEEVNELQYRQ 120
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-ARRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114 121 EQLELLITNLMRQVDR----------LKEEKEEREKEAVSYYNALEKARVAN----QDLQVQLDQALQQALDPNSKGNSL 186
Cdd:COG4942   100 EAQKEELAELLRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELEAL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462603114 187 FAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATL 232
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-198 3.56e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   11 AIKQQQKMHLEKLEEQLSRSHGQ---EVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQE- 86
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEEleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEl 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   87 ------------SMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLEL-LITNLMRQVDRLKEEKEEREKEAVSYYN 153
Cdd:TIGR02168  378 eeqletlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkLEEAELKELQAELEELEEELEELQEELE 457

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2462603114  154 ALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAME 198
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
20-221 4.04e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  20 LEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLkHQVDHQKELLSCKSEELRVMSERVQESMssEMLALQIEL 99
Cdd:COG4717    51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY-AELQEELEELEEELEELEAELEELREEL--EKLEKLLQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114 100 TEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDP 179
Cdd:COG4717   128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462603114 180 NSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQ 221
Cdd:COG4717   208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 2-366 5.26e-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: 39.72  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114    2 LESLSCECEAIKQQQKMHLEKLEEQLsRSHGQEVNELKTkiekLKVELDEArlSEKQLKHQVD----HQKELLSCKSEEL 77
Cdd:pfam15921  154 LEAAKCLKEDMLEDSNTQIEQLRKMM-LSHEGVLQEIRS----ILVDFEEA--SGKKIYEHDSmstmHFRSLGSAISKIL 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   78 RvmservqeSMSSEMLALQIELTEMESMKTTLKEEvnelqyRQEQLELLitnLMRQVDRLKEEKEEREKEAVSYYNALEK 157
Cdd:pfam15921  227 R--------ELDTEISYLKGRIFPVEDQLEALKSE------SQNKIELL---LQQHQDRIEQLISEHEVEITGLTEKASS 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  158 ARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKY----QSLKKQNVFNREQMQRMKLQIATLL 233
Cdd:pfam15921  290 ARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYedkiEELEKQLVLANSELTEARTERDQFS 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  234 QMKGSQTefEQQERLLAMLEQKNGE---------------------IKHLLGEI--RNLE--KFKNLYDSMESKPsvdSG 288
Cdd:pfam15921  370 QESGNLD--DQLQKLLADLHKREKElslekeqnkrlwdrdtgnsitIDHLRRELddRNMEvqRLEALLKAMKSEC---QG 444

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  289 TLEDNTYY----TDLLQmKLDNLNKEIESTK-------GELSIQRMkALFESQRAL-DIERKLFANERCLQLSESENMKL 356
Cdd:pfam15921  445 QMERQMAAiqgkNESLE-KVSSLTAQLESTKemlrkvvEELTAKKM-TLESSERTVsDLTASLQEKERAIEATNAEITKL 522

                          410
                   ....*....|
gi 2462603114  357 RAKLDeLKLK 366
Cdd:pfam15921  523 RSRVD-LKLQ 531
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
33-214 5.27e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  33 QEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSckseelRVMSERVQESMSSEMLALQIELTEMESMKTTLKEE 112
Cdd:COG3206   219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP------ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPD 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114 113 VNELQYRQEQLELLITNLMRQVdrlkeekeerekeAVSYYNALEKARVANQDLQVQLDQALQQALDpnskgnslFAEVED 192
Cdd:COG3206   293 VIALRAQIAALRAQLQQEAQRI-------------LASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEA 351

                         170       180
                  ....*....|....*....|..
gi 2462603114 193 RRAAMERQLISMKVKYQSLKKQ 214
Cdd:COG3206   352 ELRRLEREVEVARELYESLLQR 373
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 4-265 5.49e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114    4 SLSCECEaIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSER 83
Cdd:TIGR00618  581 RSKEDIP-NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   84 VQESMSS----EMLALQI---ELTEMESMKTTLKEEVNELQYRQEQLELLITNLmRQVDRLKEEKEEREKEAVSYYNale 156
Cdd:TIGR00618  660 VREHALSirvlPKELLASrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLA--- 735

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  157 karvANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISmkvKYQSLKKQNVFNREQMQRMKLQIATL---- 232
Cdd:TIGR00618  736 ----AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA---ELSHLAAEIQFFNRLREEDTHLLKTLeaei 808

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462603114  233 ------------LQMKGSQTEFEQQERLLAMLEQKNGEIKHLLGE 265
Cdd:TIGR00618  809 gqeipsdedilnLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 91-366 5.50e-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: 5.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114   91 EMLALQIELTEMEsmKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAvsyyNALEKARVANQDLQVQLD 170
Cdd:TIGR02168  687 EELEEKIAELEKA--LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV----EQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  171 QALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQ-MKGSQTEFEQQERLL 249
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErLESLERRIAATERRL 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462603114  250 AMLEQkngEIKHLLGEIRNLEKfknlydSMEskpsvDSGTLEDNtyytdlLQMKLDNLNKEIESTKGELSIQRMKALFES 329
Cdd:TIGR02168  841 EDLEE---QIEELSEDIESLAA------EIE-----ELEELIEE------LESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2462603114  330 QRALDIERKLFANERCLQLSESENMKLRAKLDELKLK 366
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
 
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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