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Conserved domains on  [gi|767973427|ref|XP_011536312|]
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keratin, type II cytoskeletal 78 isoform X1 [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 12177240)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
110-391 1.99e-91

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 281.04  E-value: 1.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  110 QETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKA 189
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  190 CRDQEEEYKSKYEEEAHRRATLENDFVVLKK--------------------------------ELGQLQTQASDTSVVLS 237
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKdldeatlarvdleakieslkeelaflkknheeEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  238 MDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQ 317
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973427  318 NASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 391
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
43-107 4.53e-18

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 81.24  E-value: 4.53e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427   43 SFGGCleGSRGSTWGSGGRLGVRFGE----WSGGPGLSLCPPGGIQEVTINQNLLTPLKIEIDPQFQVV 107
Cdd:pfam16208  90 GFGGG--GGFGGGFGGGGYGGGGFGGggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
110-391 1.99e-91

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 281.04  E-value: 1.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  110 QETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKA 189
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  190 CRDQEEEYKSKYEEEAHRRATLENDFVVLKK--------------------------------ELGQLQTQASDTSVVLS 237
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKdldeatlarvdleakieslkeelaflkknheeEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  238 MDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQ 317
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973427  318 NASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 391
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
43-107 4.53e-18

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 81.24  E-value: 4.53e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427   43 SFGGCleGSRGSTWGSGGRLGVRFGE----WSGGPGLSLCPPGGIQEVTINQNLLTPLKIEIDPQFQVV 107
Cdd:pfam16208  90 GFGGG--GGFGGGFGGGGYGGGGFGGggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-389 7.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 7.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERG------ALDAELKACRdqeeeykskYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMD 239
Cdd:COG1196  195 LGELERQLEPLERQAEkaeryrELKEELKELE---------AELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 240 NNRYLDFSSIITEVRARYEEiarssKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNA 319
Cdd:COG1196  266 EAELEELRLELEELELELEE-----AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973427 320 SLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEE 389
Cdd:COG1196  341 ELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-386 1.10e-08

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: 57.76  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMDNNRYLD 245
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   246 FSSIITEVRARYEEiARSSKAEAEALYQT---KYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQ 322
Cdd:TIGR02168  759 LEAEIEELEERLEE-AEEELAEAEAEIEEleaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973427   323 AAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLE 386
Cdd:TIGR02168  838 RRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
PRK09039 PRK09039
peptidoglycan -binding protein;
220-359 9.64e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 9.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 220 KELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARyeeiARSSKAEAEALyQTKYQELQVSAQLHGDRMQETKVQISQ 299
Cdd:PRK09039  53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS----LSAAEAERSRL-QALLAELAGAGAAAEGRAGELAQELDS 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973427 300 LHQEIQR-------LQSQTENLKKQNASLQAAITDAEQRGelalKDAQAKVD----ELEAALRMAKQNLAR 359
Cdd:PRK09039 128 EKQVSARalaqvelLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
110-391 1.99e-91

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 281.04  E-value: 1.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  110 QETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWhLLQQQGLSGSQQGLEPVFEACLDQLRKQLEQLQGERGALDAELKA 189
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKI-SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  190 CRDQEEEYKSKYEEEAHRRATLENDFVVLKK--------------------------------ELGQLQTQASDTSVVLS 237
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKdldeatlarvdleakieslkeelaflkknheeEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  238 MDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQ 317
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973427  318 NASLQAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEECR 391
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
43-107 4.53e-18

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 81.24  E-value: 4.53e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427   43 SFGGCleGSRGSTWGSGGRLGVRFGE----WSGGPGLSLCPPGGIQEVTINQNLLTPLKIEIDPQFQVV 107
Cdd:pfam16208  90 GFGGG--GGFGGGFGGGGYGGGGFGGggfgGRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-389 7.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 7.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERG------ALDAELKACRdqeeeykskYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMD 239
Cdd:COG1196  195 LGELERQLEPLERQAEkaeryrELKEELKELE---------AELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 240 NNRYLDFSSIITEVRARYEEiarssKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNA 319
Cdd:COG1196  266 EAELEELRLELEELELELEE-----AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973427 320 SLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEE 389
Cdd:COG1196  341 ELEEELEEAEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 163-383 7.74e-09

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: 57.47  E-value: 7.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMDNNR 242
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 243 YLDFssiiteVRARYeeiaRSSKAEAEA--LYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNAS 320
Cdd:COG4942  106 LAEL------LRALY----RLGRQPPLAllLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973427 321 LQAAITD-AEQRGEL--ALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRR 383
Cdd:COG4942  176 LEALLAElEEERAALeaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 166-386 1.10e-08

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: 57.76  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMDNNRYLD 245
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   246 FSSIITEVRARYEEiARSSKAEAEALYQT---KYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQ 322
Cdd:TIGR02168  759 LEAEIEELEERLEE-AEEELAEAEAEIEEleaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973427   323 AAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLE 386
Cdd:TIGR02168  838 RRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-389 2.34e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 163 EACLDQLRKQLEQLQGERGALDAEL-------KACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVV 235
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELeelrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 236 LSMDNNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLhgdrmQETKVQISQLHQEIQRLQSQTENLK 315
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAEELLEALRAAAELA 399

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973427 316 KQNASLQAAITDAEQR---GELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEE 389
Cdd:COG1196  400 AQLEELEEAEEALLERlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-367 5.44e-08

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: 55.45  E-value: 5.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   107 VRTQETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWHLLQQQGLSGSQQGLEP------------VFEACLDQLRKQLE 174
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrkdlaRLEAEVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   175 QLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMDNNRYLDfssiITEVR 254
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN----LRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   255 ARYEEIARSSKAEAEALYQTKYQELQvsaqlhgdRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGEL 334
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSE--------DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 767973427   335 A---LKDAQAKVDELEAALRMAKQNLARLLCEYQEL 367
Cdd:TIGR02168  899 LseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 206-383 9.28e-08

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: 55.06  E-value: 9.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   206 HRRATLENDFVVLKKELGQLQTQASdtsvVLSMD--NNRYLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSA 283
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELELALL----VLRLEelREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   284 QLHG--DRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELA---LKDAQAKVDELEAALRMAKQNLA 358
Cdd:TIGR02168  282 EIEElqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELE 361

                          170       180
                   ....*....|....*....|....*
gi 767973427   359 RLLCEYQELTSTKLSLDVEIATYRR 383
Cdd:TIGR02168  362 ELEAELEELESRLEELEEQLETLRS 386
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
166-371 6.00e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.94  E-value: 6.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAH--RRATLENDFVVLKKELGQLQTQASDTSVVLSMDNN-- 241
Cdd:COG3206  177 LEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDal 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 242 RYLDFSSIITEVRARYEEiARSSKAEAEALYQTKYQELQvSAQlhgDRMQETKVQISQLHQEI-QRLQSQTENLKKQNAS 320
Cdd:COG3206  257 PELLQSPVIQQLRAQLAE-LEAELAELSARYTPNHPDVI-ALR---AQIAALRAQLQQEAQRIlASLEAELEALQAREAS 331

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767973427 321 LQAAITDAEQRGeLALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTK 371
Cdd:COG3206  332 LQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-386 7.52e-07

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: 51.99  E-value: 7.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   162 FEACLDQLRKQLEQLQGERgaLDAE----LKACRDQEEEYKSKYEEEAHRR--ATLENDFVVLKKELGQLQTQASD---- 231
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRRER--EKAEryqaLLKEKREYEGYELLKEKEALERqkEAIERQLASLEEELEKLTEEISElekr 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   232 -----------TSVVLSMDNNRYLDFSSIITEVRAryeEIARSSKAEAEalyqtKYQELQVSAQlhgdRMQETKVQISQL 300
Cdd:TIGR02169  267 leeieqlleelNKKIKDLGEEEQLRVKEKIGELEA---EIASLERSIAE-----KERELEDAEE----RLAKLEAEIDKL 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   301 HQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIat 380
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL-- 408


                   ....*.
gi 767973427   381 yRRLLE 386
Cdd:TIGR02169  409 -DRLQE 413
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
212-360 8.91e-07

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 50.82  E-value: 8.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 212 ENDFVvlKKelGQlqtqasdtsVVLSMDNNRYLdfsSIITEVRARYEEiARSSKAEAEALYQTKYQELQVSAQLHGDRMQ 291
Cdd:COG1566   63 EGDRV--KK--GQ---------VLARLDPTDLQ---AALAQAEAQLAA-AEAQLARLEAELGAEAEIAAAEAQLAAAQAQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 292 ETKVQ--------------ISQlhQEIQRLQSQTENLKKQNASLQAAITDAEQ--RGELALKDAQAKVDELEAALRMAKQ 355
Cdd:COG1566  126 LDLAQreleryqalykkgaVSQ--QELDEARAALDAAQAQLEAAQAQLAQAQAglREEEELAAAQAQVAQAEAALAQAEL 203


                 ....*
gi 767973427 356 NLARL 360
Cdd:COG1566  204 NLART 208
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-360 2.79e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMDNNRYLD 245
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 246 FSSIITEVRARYEEIARSSKAEAEAL--YQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQA 323
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767973427 324 AITDAEQRGELALKDAQAKVDELEAALRMAKQNLARL 360
Cdd:COG1196  471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 169-380 2.95e-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: 50.07  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   169 LRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLSMDNNRYL-DFS 247
Cdd:TIGR02169  721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqAEL 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   248 SIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHgDRMQETKVQISQLHQEIqrlqsqtENLKKQNASLQAAItd 327
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ-EQRIDLKEQIKSIEKEI-------ENLNGKKEELEEEL-- 870

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973427   328 AEQRGELA-----LKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIAT 380
Cdd:TIGR02169  871 EELEAALRdlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-386 5.48e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  170 RKQLEQLQGERGALDAELKACRDQEEEykskyeeeahrratlendfvvLKKELGQLQTQASDTSVVLSMDNNRyLDFSSI 249
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEA---------------------LEAELDALQERREALQRLAEYSWDE-IDVASA 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  250 ITEVRARYEEIAR--SSKAEAEALYQtKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASL-----Q 322
Cdd:COG4913   667 EREIAELEAELERldASSDDLAALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarL 745

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973427  323 AAITDAEQRGELALKDA---------QAKVDELEAALRMAKQNLARLLCEYQEL-TSTKLSLDVEIAT---YRRLLE 386
Cdd:COG4913   746 ELRALLEERFAAALGDAverelrenlEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 168-386 6.88e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.56  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  168 QLRKQLEQLQGERGALDAELKacRDQEEEYKSKYEEEAHRRA----TLENDFVVLKKELGQLQTQAsdtsvvLSMDNNRY 243
Cdd:pfam05483  82 KLYKEAEKIKKWKVSIEAELK--QKENKLQENRKIIEAQRKAiqelQFENEKVSLKLEEEIQENKD------LIKENNAT 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  244 LDFSSIITEVRARYEEIARSSKAEAEALYQ-------------TKYQELQVSAQlhgDRMQETKVQISQLHQEIQRL--- 307
Cdd:pfam05483 154 RHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekmiLAFEELRVQAE---NARLEMHFKLKEDHEKIQHLeee 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  308 -QSQTENLKKQNASLQAAITDAEQRGE---LALKDAQAKVDELEAALRMAKQNLARLLCEYQELTS----TKLSLDVEIA 379
Cdd:pfam05483 231 yKKEINDKEKQVSLLLIQITEKENKMKdltFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKeledIKMSLQRSMS 310


                  ....*..
gi 767973427  380 TYRRLLE 386
Cdd:pfam05483 311 TQKALEE 317
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 279-385 9.55e-06

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: 47.84  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 279 LQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLA 358
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86

                         90       100
                 ....*....|....*....|....*..
gi 767973427 359 RLLceyQELTSTKLSLDVEIATYRRLL 385
Cdd:COG4942   87 ELE---KEIAELRAELEAQKEELAELL 110
PRK09039 PRK09039
peptidoglycan -binding protein;
220-359 9.64e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 9.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 220 KELGQLQTQASDTSVVLSMDNNRYLDFSSIITEVRARyeeiARSSKAEAEALyQTKYQELQVSAQLHGDRMQETKVQISQ 299
Cdd:PRK09039  53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRAS----LSAAEAERSRL-QALLAELAGAGAAAEGRAGELAQELDS 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973427 300 LHQEIQR-------LQSQTENLKKQNASLQAAITDAEQRGelalKDAQAKVD----ELEAALRMAKQNLAR 359
Cdd:PRK09039 128 EKQVSARalaqvelLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-342 2.53e-05

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: 46.30  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVLS-------- 237
Cdd:COG4942   36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAellralyr 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 238 MDNNRYLDF-----SSIITEVRARY-EEIARSSKAEAEALYQTKYQELQVSAQLHGDR--------------------MQ 291
Cdd:COG4942  116 LGRQPPLALllspeDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERaeleallaeleeeraalealKA 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767973427 292 ETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRGELALKDAQAK 342
Cdd:COG4942  196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-386 2.56e-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: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  166 LDQLRKQLEQLQGERgALDAELKACRDQEEEYKSKYEEEAHRRATLENDfvVLKKELGQLQTQASDTSvvlsmdnnryld 245
Cdd:COG4913   244 LEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLE------------ 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  246 fssiitevraryEEIARSSKAEAEAlyQTKYQELQVS-AQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASL--- 321
Cdd:COG4913   309 ------------AELERLEARLDAL--REELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglp 374

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973427  322 -----------QAAITDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLE 386
Cdd:COG4913   375 lpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
167-367 2.62e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 167 DQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENdfvvLKKELGQL----QTQasdtsvVLSMDNNR 242
Cdd:COG1340   67 DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDK----LRKEIERLewrqQTE------VLSPEEEK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 243 ylDFSSIITEVRARYEEI--ARSSKAEAEALYqTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNAS 320
Cdd:COG1340  137 --ELVEKIKELEKELEKAkkALEKNEKLKELR-AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767973427 321 LQAAItdaeqrgelalKDAQAKVDELEAALRMAKQNLARLLCEYQEL 367
Cdd:COG1340  214 LHKEI-----------VEAQEKADELHEEIIELQKELRELRKELKKL 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
163-353 2.67e-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: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRR-ATLENDFVVLKKELGQLQTQASD-----TSVVL 236
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARleallAALGL 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  237 SMDNNRyLDFSSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHgdrmqetkvqisQLHQEIQRLQSQTENLKK 316
Cdd:COG4913   374 PLPASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR------------ELEAEIASLERRKSNIPA 440

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767973427  317 QNASLQAAITDAeqrgeLALKDAQAK-------VDELEAALRMA 353
Cdd:COG4913   441 RLLALRDALAEA-----LGLDEAELPfvgelieVRPEEERWRGA 479
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 163-388 3.48e-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: 46.60  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQasdtsvvlsmdnnr 242
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE-------------- 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   243 yldfssiITEVRARYEEIARSSKAEAEAL--YQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNAS 320
Cdd:TIGR02169  373 -------LEEVDKEFAETRDELKDYREKLekLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973427   321 LQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARLlceYQELTSTKLSLDVEIATYRRLLEGE 388
Cdd:TIGR02169  446 KALEIKKQEWK----LEQLAADLSKYEQELYDLKEEYDRV---EKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-360 3.87e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 3.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   112 TQEIRTLNNQFASFIDKVRFLEQQNKVLETKWHLLQQQGLSGsqqglepvfEACLDQLRKQLEQLQGERGALDAELKACR 191
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL---------AEELAELEEKLEELKEELESLEAELEELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   192 DQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQasdtsvvlsmdnnryldfssiITEVRARYEEIARSskaeaeaL 271
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNE---------------------IERLEARLERLEDR-------R 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427   272 YQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAALR 351
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ----ALDAAERELAQLQARLD 492


                   ....*....
gi 767973427   352 MAKQNLARL 360
Cdd:TIGR02168  493 SLERLQENL 501
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 166-367 1.18e-04

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: 43.37  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERGALDAELKACRDqeeeykskyeeeahRRATLENDFVVLKKELGQLQTQasdtsvvlsmdnnryld 245
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEA--------------RLEAAKTELEDLEKEIKRLELE----------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 246 fssiITEVRARyeeIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAI 325
Cdd:COG1579   68 ----IEEVEAR---IKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767973427 326 TDAEQRGELALKDAQAKVDELEAALRMAKQNL-ARLLCEYQEL 367
Cdd:COG1579  141 EEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERI 183
GrpE COG0576
Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein ...
 290-356 3.01e-04

Molecular chaperone GrpE (heat shock protein HSP-70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440341 [Multi-domain]  Cd Length: 147  Bit Score: 40.91  E-value: 3.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973427 290 MQETKVQISQLHQEIQRLQSQTENLKKQnaslqaaitdAEQRGELALKDAQAKV--------DELEAALRMAKQN 356
Cdd:COG0576    1 MEELEAELAELKDRLLRLQAEFENYRKR----------TEREREEARKYALEKLaedllpvlDNLERALAAAEED 65
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
250-360 3.43e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 250 ITEVRARYEEI-ARSSKAEAEALYQTKYQEL-QVSAQLHG--DRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAI 325
Cdd:COG4717  104 LEELEAELEELrEELEKLEKLLQLLPLYQELeALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELL 183

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767973427 326 TDAEQRGELALKDAQAKVDELEAALRMAKQNLARL 360
Cdd:COG4717  184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 110-359 5.33e-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: 42.06  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 110 QETQEIRTLNNQFASFIDKVRFLEQQNKVLETKWHLLqqqglsgsqqglepvfEACLDQLRKQLEQLQGERGALDAELKA 189
Cdd:COG4942   38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----------------EQELAALEAELAELEKEIAELRAELEA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 190 CRDQeeeykskyeeeahrratlendfvvLKKELGQLQTQASDTSVVLSMDNNRYLDFSSIItevrARYEEIARSSKAEAE 269
Cdd:COG4942  102 QKEE------------------------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 270 ALYQTKyQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAA 349
Cdd:COG4942  154 ELRADL-AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEAL 228

                        250
                 ....*....|
gi 767973427 350 LRMAKQNLAR 359
Cdd:COG4942  229 IARLEAEAAA 238
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 205-358 6.10e-04

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 42.02  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  205 AHRRATLENDFVVLKKELG-QLQTQASDTSVVLSMDNNRYLDFSSI-ITEVRARYEEIARSSKAEAEAlyQTKYQELQvs 282
Cdd:TIGR04320 199 GHAQNLLGDDKINAGAYLGvSISNDGGVTIHFVNFNDSYIADGNKFdKTPIPNPPNSLAALQAKLATA--QADLAAAQ-- 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973427  283 aqlhgDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAitdAEQRGELALKDAQAKVDELEAALRMAKQNLA 358
Cdd:TIGR04320 275 -----TALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQ---ALQTAQNNLATAQAALANAEARLAKAKEALA 342
PRK12704 PRK12704
phosphodiesterase; Provisional
 247-360 1.77e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 247 SSIITEVRARYEEIARSSKAEA-----EALYQTKYQELQVSAQLHGD---RMQETKVQISQLHQEIQRLQSQTENLKKQN 318
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEAeaikkEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRLLQKEENLDRKLELLEKRE 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767973427 319 ASLQAAITDAEQRgELALKDAQAKVDELEAALRMAKQNLARL 360
Cdd:PRK12704 110 EELEKKEKELEQK-QQELEKKEEELEELIEEQLQELERISGL 150
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 296-360 1.97e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.84  E-value: 1.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973427  296 QISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALRMAKQNLARL 360
Cdd:pfam11559  60 TIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
163-385 2.63e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASDTSVVlsmDNNR 242
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAI---ADAE 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 243 yldfsSIITEVRARYEEIARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQ 322
Cdd:PRK02224 606 -----DEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427 323 AAITDAEqrGELA-LKDAQAKVDELEAALrmakQNLARLLCEYQELTSTKLSLDVE-----IATYRRLL 385
Cdd:PRK02224 681 AEIGAVE--NELEeLEELRERREALENRV----EALEALYDEAEELESMYGDLRAElrqrnVETLERML 743
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 271-359 2.77e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 39.93  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 271 LYQTKYQELQVSAQLhgdRMQETKVQISQLHQEIQRLQSqtenLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAAL 350
Cdd:COG0845   54 LDPPDLQAALAQAQA---QLAAAQAQLELAKAELERYKA----LLKKGAVSQQELDQAKA----ALDQAQAALAAAQAAL 122


                 ....*....
gi 767973427 351 RMAKQNLAR 359
Cdd:COG0845  123 EQARANLAY 131
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 273-351 3.61e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 3.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427 273 QTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRgelaLKDAQAKVDELEAALR 351
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELG 89
OEP pfam02321
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ...
 244-361 3.99e-03

Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.


Pssm-ID: 396757 [Multi-domain]  Cd Length: 181  Bit Score: 38.27  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  244 LDFSSIITEVRAryeeiARSSKAEAEALYQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQA 323
Cdd:pfam02321  69 FDGGKRRARVKA-----AKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLI 143

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767973427  324 AITDAEQrGELALKDAQAKVDELEAALRMAKQNLARLL 361
Cdd:pfam02321 144 SLLDVLQ-AEVELLEARLELLNAEADLELALAQLEQLL 180
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
126-366 4.23e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 126 IDKVRFLEQQNKVLETKWHLLQQQGLSGSQQGLEPVFEACLDQlrKQLEQLQGERGALDAELKacrdqeeeyksKYEEEA 205
Cdd:COG4717  304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI--EELQELLREAEELEEELQ-----------LEELEQ 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 206 HRRATLENDFVVLKKELGQLQTQAsdtsvvlsmdnNRYLDFSSIITEVRARYEEIARSSKAEAEALY----QTKYQELQv 281
Cdd:COG4717  371 EIAALLAEAGVEDEEELRAALEQA-----------EEYQELKEELEELEEQLEELLGELEELLEALDeeelEEELEELE- 438

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 282 saqlhgDRMQETKVQISQLHQEIQRLQSQTENLKKQNaslqaAITDAEQRGELALKDAQAKVDELeAALRMAKQNLARLL 361
Cdd:COG4717  439 ------EELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEW-AALKLALELLEEAR 506


                 ....*
gi 767973427 362 CEYQE 366
Cdd:COG4717  507 EEYRE 511
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
166-396 4.29e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQ------------LQGERGALDAELKACRDQEEEYkskyeeeahrRATLENDFVVL------KKELGQLQT 227
Cdd:PRK02224 189 LDQLKAQIEEkeekdlherlngLESELAELDEEIERYEEQREQA----------RETRDEADEVLeeheerREELETLEA 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 228 QASDTSVVLSMDNNRYLDFSSIITEVRARYEEIARS----------SKAEAEAL------YQTKYQELQVSAQLHGDRMQ 291
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeaglDDADAEAVearreeLEDRDEELRDRLEECRVAAQ 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 292 ETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDA-----EQRGELA-----LKDAQAKVDELEAALRMAKQNLARLL 361
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAreaveDRREEIEeleeeIEELRERFGDAPVDLGNAEDFLEELR 418

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 767973427 362 CEYQELTSTKLSLDVEIATYR-RLLEGEECRMSGEC 396
Cdd:PRK02224 419 EERDELREREAELEATLRTAReRVEEAEALLEAGKC 454
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 160-360 4.46e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.33  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  160 PVFEACLDQLRKQLEQLQGERGALDAELKacrdqeeeykskyeeeahRRATLENDFVVLKKELGQLQTQASDTSVVLSmD 239
Cdd:pfam00529  54 TDYQAALDSAEAQLAKAQAQVARLQAELD------------------RLQALESELAISRQDYDGATAQLRAAQAAVK-A 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  240 NNRYLDFSSII---TEVRARYEEIARSSKAEAEALYQtkyqelQVSAQLhgdrmQETKVQISQLHQEIqrLQSQTENLkk 316
Cdd:pfam00529 115 AQAQLAQAQIDlarRRVLAPIGGISRESLVTAGALVA------QAQANL-----LATVAQLDQIYVQI--TQSAAENQ-- 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767973427  317 qnaslqaaitdAEQRGELAlkDAQAKVDELEAALRMAKQNLARL 360
Cdd:pfam00529 180 -----------AEVRSELS--GAQLQIAEAEAELKLAKLDLERT 210
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
245-383 4.57e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 245 DFSSIITEVRARYEEIARSSKAEAEaLYQTKYQELQVSAQLHGDRMQEtkvQISQLHQEIQRLQSQTENLKKQNASLQAA 324
Cdd:COG4717  386 ELRAALEQAEEYQELKEELEELEEQ-LEELLGELEELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAE 461

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427 325 ITDAEQRGELAlkdaqakvdELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRR 383
Cdd:COG4717  462 LEQLEEDGELA---------ELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
Phage_GP20 pfam06810
Phage minor structural protein GP20; This family consists of several phage minor structural ...
 280-354 5.71e-03

Phage minor structural protein GP20; This family consists of several phage minor structural protein GP20 sequences of around 180 residues in length. The function of this family is unknown.


Pssm-ID: 429131 [Multi-domain]  Cd Length: 149  Bit Score: 37.34  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  280 QVSAQLHGD-----RMQETKVQISQLHQEIQRLQSQTENLKKQ---NASLQAAITDAEQRGELALKDAQAKV------DE 345
Cdd:pfam06810   5 KVMEAENGKdipkaKFDEVNTERDTLKEQLATRDKQLKDLKKVakdNEELQKQIDELQAKNKDAEADYEAKIadlkfdNA 84


                  ....*....
gi 767973427  346 LEAALRMAK 354
Cdd:pfam06810  85 IKLALKGAK 93
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
166-389 6.36e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 166 LDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQASdtsvvlsmdnnryld 245
Cdd:COG4372   47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE--------------- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 246 fssiitEVRARYEEIarssKAEAEALYQTKyQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAi 325
Cdd:COG4372  112 ------ELQEELEEL----QKERQDLEQQR-KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA- 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973427 326 tDAEQRGELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATYRRLLEGEE 389
Cdd:COG4372  180 -EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 167-378 7.58e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.88  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  167 DQLRKQLEQLQGERGALDAElkacrdQEEEYKSKYEEEAHRRATLE---------NDFVVLKKELGQLQTQASDT--SVV 235
Cdd:PRK10929   26 KQITQELEQAKAAKTPAQAE------IVEALQSALNWLEERKGSLErakqyqqviDNFPKLSAELRQQLNNERDEprSVP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427  236 LSMDNNrylDFSSIITEVRARYEEIARSSKAEaealyQTKYQELQVSAQLHGDRMQETKVQISQLHQEIQRLQSQTENLK 315
Cdd:PRK10929  100 PNMSTD---ALEQEILQVSSQLLEKSRQAQQE-----QDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973427  316 K-QNASLQAaitdaeqrgELALKdaQAKVDELEAALRMA--KQNLARLLCEYQELTSTKLSLDVEI 378
Cdd:PRK10929  172 QaQLTALQA---------ESAAL--KALVDELELAQLSAnnRQELARLRSELAKKRSQQLDAYLQA 226
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
262-361 7.69e-03

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 38.48  E-value: 7.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 262 RSSKAEAEALYQTKYQELQvsaqlhgDRMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQRG--------- 332
Cdd:COG1538   50 RARIEAAKAQAEAAEADLR-------AARLDLAAEVAQAYFDLLAAQEQLALAEENLALAEELLELARARYeaglasrld 122

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767973427 333 ----ELALKDAQAKVDELEAALRMAKQNLARLL 361
Cdd:COG1538  123 vlqaEAQLAQARAQLAQAEAQLAQARNALALLL 155
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 163-381 8.28e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 163 EACLDQLRKQLEQLQGERGALDAELKACRDQEEEYKSKYEEEAHRRATLENDFVVLKKELGQLQTQasdtsvvlsmdnnr 242
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE-------------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973427 243 yldfssiITEVRARYEEIARsskaeaeALYQTKYQELQVSAQLHG-------DRMQETKVQISQLHQEIQRLQSQTENLK 315
Cdd:COG3883   81 -------IEERREELGERAR-------ALYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELE 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973427 316 KQNASLQAAITDAEQRG---ELALKDAQAKVDELEAALRMAKQNLARLLCEYQELTSTKLSLDVEIATY 381
Cdd:COG3883  147 AKKAELEAKLAELEALKaelEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 289-360 9.18e-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: 37.60  E-value: 9.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973427 289 RMQETKVQISQLHQEIQRLQSQTENLKKQNASLQAAITDAEQrgelALKDAQAKVDELEAALRMAKQNLARL 360
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEEVEARIKKY 78
 
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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