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Conserved domains on  [gi|133778953|ref|NP_032501|]
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keratin, type II cytoskeletal 4 [Mus musculus]

Protein Classification

type II keratin( domain architecture ID 12177255)

type II keratin is an intermediate filament-forming protein that provides mechanical support and fulfills a variety of additional functions in epithelial cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-458 3.14e-148

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 427.41  E-value: 3.14e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953  386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 2.12e-27

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.82  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   14 GFSSGSAIAGGVKRVAFSSGSM------SGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGA 87
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSsrrgggGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778953   88 GFGAGGFGGGFGGSFNG---------------------RGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GGFGGGGGGGFGGGGGFgggfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-458 3.14e-148

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 427.41  E-value: 3.14e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953  386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 2.12e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.82  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   14 GFSSGSAIAGGVKRVAFSSGSM------SGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGA 87
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSsrrgggGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778953   88 GFGAGGFGGGFGGSFNG---------------------RGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GGFGGGGGGGFGGGGGFgggfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-427 4.75e-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: 55.83  E-value: 4.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   144 TAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLqqqttttspKSLDPFFETYINALRKNLDTLSNDKGRLQSELK 223
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------RLEVSELEEEIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   224 MMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEInftrvlyEAELAQMQthvsdtsvvl 303
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELE---------- 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   304 smdnnrnlDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQH--GDSLKTTKNEISELNRMIQR-----LRA 376
Cdd:TIGR02168  369 --------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRRERLQQEIEELLKKLEEaelkeLQA 440

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 133778953   377 EIENIKKQSQTLQASVADAEQRGELALKdaysKRAELETALQKAKEDLARL 427
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELRE----ELEEAEQALDAAERELAQL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-456 5.49e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINf 280
Cdd:COG1196  255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE- 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 281 trvLYEAELAQMQTHVSDTSVVLSMDNNRnldldgiIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQhgdslKTT 360
Cdd:COG1196  334 ---ELEEELEELEEELEEAEEELEEAEAE-------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 361 KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQ---RGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                        250
                 ....*....|....*....
gi 133778953 438 KLALDVEIATYRKLLEGEE 456
Cdd:COG1196  479 LAELLEELAEAAARLLLLL 497
46 PHA02562
endonuclease subunit; Provisional
 162-414 4.12e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.24  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 162 DKVRFLEQQNKVLETKWNLLQQQTTTtspksldpfFETYINALRKnldtLSNDKgrlQSELKMMQDSVEDFKTKYEEEIN 241
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRK----KNGEN---IARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 242 KRTAAENDFVVLKKDVDAAY----MIKVELEAKMESLKDEINFTRVLYEAElAQMQThvsdtsvvLSMDNNRNLDLDGII 317
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCP-TCTQQ--------ISEGPDRITKIKDKL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 318 AEVRAQYEDIarkskaeveswyQIKVQQLQMSADQHGD---SLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVAD 394
Cdd:PHA02562 309 KELQHSLEKL------------DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376

                        250       260
                 ....*....|....*....|....*
gi 133778953 395 AEqrGELA-----LKDAYSKRAELE 414
Cdd:PHA02562 377 NA--EELAklqdeLDKIVKTKSELV 399
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-458 3.14e-148

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 427.41  E-value: 3.14e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA-EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953  386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 2.12e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.82  E-value: 2.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   14 GFSSGSAIAGGVKRVAFSSGSM------SGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVGGYGA 87
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSsrrgggGGGGGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGGGGGFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778953   88 GFGAGGFGGGFGGSFNG---------------------RGGPGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GGFGGGGGGGFGGGGGFgggfggggyggggfggggfggRGGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-427 4.75e-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: 55.83  E-value: 4.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   144 TAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLqqqttttspKSLDPFFETYINALRKNLDTLSNDKGRLQSELK 223
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------RLEVSELEEEIEELQKELYALANEISRLEQQKQ 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   224 MMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEInftrvlyEAELAQMQthvsdtsvvl 303
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-------EELEAELE---------- 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   304 smdnnrnlDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQH--GDSLKTTKNEISELNRMIQR-----LRA 376
Cdd:TIGR02168  369 --------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRRERLQQEIEELLKKLEEaelkeLQA 440

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 133778953   377 EIENIKKQSQTLQASVADAEQRGELALKdaysKRAELETALQKAKEDLARL 427
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELRE----ELEEAEQALDAAERELAQL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-456 5.49e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINf 280
Cdd:COG1196  255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE- 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 281 trvLYEAELAQMQTHVSDTSVVLSMDNNRnldldgiIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQhgdslKTT 360
Cdd:COG1196  334 ---ELEEELEELEEELEEAEEELEEAEAE-------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-----AEL 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 361 KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQ---RGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                        250
                 ....*....|....*....
gi 133778953 438 KLALDVEIATYRKLLEGEE 456
Cdd:COG1196  479 LAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 313-450 7.69e-07

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: 51.98  E-value: 7.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   313 LDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHG--DSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQA 390
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953   391 SVADAEQRGELALKDAYSKRAELETALQK---AKEDLARLLRDYQALMNVKLALDVEIATYRK 450
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRS 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-453 3.11e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   217 RLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINftrvlyeaELAQMQTHV 296
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--------QLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   297 SDTsvvlsmdnnrNLDLDGIIAEVRAQYEDiARKSKAEVESwyqiKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRA 376
Cdd:TIGR02168  753 SKE----------LTELEAEIEELEERLEE-AEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   377 EIENIKKQSQTLQASVADAEQRGELA---LKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLE 453
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
46 PHA02562
endonuclease subunit; Provisional
 162-414 4.12e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.24  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 162 DKVRFLEQQNKVLETKWNLLQQQTTTtspksldpfFETYINALRKnldtLSNDKgrlQSELKMMQDSVEDFKTKYEEEIN 241
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRK----KNGEN---IARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 242 KRTAAENDFVVLKKDVDAAY----MIKVELEAKMESLKDEINFTRVLYEAElAQMQThvsdtsvvLSMDNNRNLDLDGII 317
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCP-TCTQQ--------ISEGPDRITKIKDKL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 318 AEVRAQYEDIarkskaeveswyQIKVQQLQMSADQHGD---SLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVAD 394
Cdd:PHA02562 309 KELQHSLEKL------------DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376

                        250       260
                 ....*....|....*....|....*
gi 133778953 395 AEqrGELA-----LKDAYSKRAELE 414
Cdd:PHA02562 377 NA--EELAklqdeLDKIVKTKSELV 399
PRK01156 PRK01156
chromosome segregation protein; Provisional
 134-456 1.36e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.97  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 134 EIDPEIQKIRTAE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQT------TTTSPKSLDPFFETY---INA 203
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHYnekKSR 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 204 LRKNLDTLSNDKGRLQSE---LKMMQDSVEDFKT-KYEEEINKRTAAENDfvvLKKDVDAAYMIKvELEAKMESLKDEIN 279
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEInKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 280 FTRVlyeAELAQMQTHVSDTSVVLSmdnnrNLDLDGIIA---EVRAQYEDIARKSK------AEVESWYQIKVQQLqmsa 350
Cdd:PRK01156 557 SLKL---EDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQeieigfPDDKSYIDKSIREI---- 624

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 351 DQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQaSVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRD 430
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703

                        330       340
                 ....*....|....*....|....*.
gi 133778953 431 YQALMNVKLALDVEIATYRKLLEGEE 456
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLESMK 729
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-436 4.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  266 ELEAKMESLKDEINFTRVLYE---AELAQMQTHVSDTSVVLSMDNNRnLDLDGI---IAEVRAQYEDIaRKSKAEVEswy 339
Cdd:COG4913   614 ALEAELAELEEELAEAEERLEaleAELDALQERREALQRLAEYSWDE-IDVASAereIAELEAELERL-DASSDDLA--- 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  340 qikvqQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALK---DAYSKRAELETA 416
Cdd:COG4913   689 -----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAV 763

                         170       180
                  ....*....|....*....|
gi 133778953  417 LQKAKEDLARLLRDYQALMN 436
Cdd:COG4913   764 ERELRENLEERIDALRARLN 783
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-453 1.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  191 KSLDPFFETY----------INALRKNLDTLSndkgRLQSELKMMQDSVE---DFKTKYEE-EINKRTAAENDFVVLKKD 256
Cdd:COG4913   207 GDLDDFVREYmleepdtfeaADALVEHFDDLE----RAHEALEDAREQIEllePIRELAERyAAARERLAELEYLRAALR 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  257 VDAAYMIKVELEAKMESLKDEINFTrvlyEAELAQMQTHVSDtsvvlsmdnnrnldLDGIIAEVRAQYEDIArkskaeve 336
Cdd:COG4913   283 LWFAQRRLELLEAELEELRAELARL----EAELERLEARLDA--------------LREELDELEAQIRGNG-------- 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  337 swyQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETA 416
Cdd:COG4913   337 ---GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 133778953  417 LQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLE 453
Cdd:COG4913   414 LRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
PRK09039 PRK09039
peptidoglycan -binding protein;
286-426 3.41e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 286 EAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDiARKSKAEVESWYQIKVQQLQMSADQHGD---SLKTTKN 362
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 133778953 363 EISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLAR 426
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
198-449 4.14e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 198 ETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKtkyeeeinkrtaAENDFVVLKKDVDAAYMIKVELEAKMESLKDE 277
Cdd:COG3206  167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 278 INFTRVLYEAELAQMQTHVSDTSVVLsmDNNRNLDLDGIIAEVRAQYEDIARKSKAEveswyQIKVQQLQmsadqhgDSL 357
Cdd:COG3206  235 LAEAEARLAALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPN-----HPDVIALR-------AQI 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 358 KTTKNEI-SELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGeLALKDAYSKRAELETALQKAKEDLARLLRDYQALmn 436
Cdd:COG3206  301 AALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEA-- 377

                        250
                 ....*....|...
gi 133778953 437 vKLALDVEIATYR 449
Cdd:COG3206  378 -RLAEALTVGNVR 389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-450 5.09e-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: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 203 ALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTR 282
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 283 vlyeAELAQMQTHVSDTSVVLSMdNNRNLDLDGIIAevRAQYEDIARKSKaevesWYQIKVQQLQmsadQHGDSLKTTKN 362
Cdd:COG4942   97 ----AELEAQKEELAELLRALYR-LGRQPPLALLLS--PEDFLDAVRRLQ-----YLKYLAPARR----EQAEELRADLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 363 EIselnrmiQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALD 442
Cdd:COG4942  161 EL-------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233


                 ....*...
gi 133778953 443 VEIATYRK 450
Cdd:COG4942  234 AEAAAAAE 241
PRK01156 PRK01156
chromosome segregation protein; Provisional
 138-427 5.45e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.97  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 138 EIQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQttttspksldpffetyINALRKNLDTLSNDKGR 217
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKE----------------IERLSIEYNNAMDDYNN 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 218 LQSELKMMQdSVEDFKTKYEEEINKrtaaendfvvLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVS 297
Cdd:PRK01156 237 LKSALNELS-SLEDMKNRYESEIKT----------AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 298 DtsvvlsMDNNRNLdLDGIIAEVRaQYEDIARKSkAEVESWYQ--IKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLR 375
Cdd:PRK01156 306 D------IENKKQI-LSNIDAEIN-KYHAIIKKL-SVLQKDYNdyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLK 376

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 133778953 376 AEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARL 427
Cdd:PRK01156 377 KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSL 428
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 201-434 5.84e-04

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: 42.80  E-value: 5.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   201 INALRKNLDTLSNDKGRLQSELKMMQDSVE----------DFKTKYEEEINKRTAA-ENDFVVLKKDVDAAYMIKVELEA 269
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaaiQGKNESLEKVSSLTAQlESTKEMLRKVVEELTAKKMTLES 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   270 KMESLKDeinFTRVLYEAELAQMQTHVSDTSVVLSMD---------NNRNLDLDGIIAEVRAQYEDIARKSKAeVESWYQ 340
Cdd:pfam15921  494 SERTVSD---LTASLQEKERAIEATNAEITKLRSRVDlklqelqhlKNEGDHLRNVQTECEALKLQMAEKDKV-IEILRQ 569

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   341 iKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIK-------KQSQTLQASVADAE-QRGEL---------AL 403
Cdd:pfam15921  570 -QIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLElEKVKLvnagserlrAV 648

                          250       260       270
                   ....*....|....*....|....*....|.
gi 133778953   404 KDAYSKRAELETALQKAKEDLARLLRDYQAL 434
Cdd:pfam15921  649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-470 8.68e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   317 IAEVRAQYEDIARK---SKAEVESwYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVA 393
Cdd:TIGR02168  679 IEELEEKIEELEEKiaeLEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   394 DAEQR----------GELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECRMSGEC 463
Cdd:TIGR02168  758 ELEAEieeleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837


                   ....*..
gi 133778953   464 KSAVSIS 470
Cdd:TIGR02168  838 RRLEDLE 844
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 125-440 1.07e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   125 QSLLTPLQVEIDPEIQKIRtAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPKSLDPffETYINAL 204
Cdd:TIGR02168  711 EEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--EAEIEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   205 RKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVL 284
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   285 YEAELAQmqthvsdtsvvlsmdnnrnldLDGIIAEVRAQYEDIARKSKAEveswyqikvQQLQMSADQHGDSLKTTKNEI 364
Cdd:TIGR02168  868 IEELESE---------------------LEALLNERASLEEALALLRSEL---------EELSEELRELESKRSELRREL 917

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778953   365 SELNRMIQRLRAEIENIKKQSQTLQASVADaeqRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLA 440
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 266-454 1.07e-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: 41.29  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 266 ELEAKMESLKDEINFT---RVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQyEDIARKSKAEVESWYQIK 342
Cdd:COG4942   31 QLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-IAELRAELEAQKEELAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 343 VQQLQMSADQHGDSLKTTKNEISELNRMIQRL-------RAEIENIKKQSQTLQASVADAE-QRGELA--LKDAYSKRAE 412
Cdd:COG4942  110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylaparREQAEELRADLAELAALRAELEaERAELEalLAELEEERAA 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 133778953 413 LETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEG 454
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 266-456 1.51e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 266 ELEAKMESLKDEINFTRVLYEAELAQMQThvsdtsvvlsmdnnrnldLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQ 345
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAE------------------LEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 346 LQMSADqhgdsLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELA---LKDAYSKRAELETALQKAKE 422
Cdd:COG1196  298 ARLEQD-----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEA 372

                        170       180       190
                 ....*....|....*....|....*....|....
gi 133778953 423 DLARLLRDYQALMNVKLALDVEIATYRKLLEGEE 456
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 199-431 1.65e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.36  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   199 TYINAlRKNLDTLSNDKgrlQSELKMMQDSVEDFKTKYEEEINKRTAAENdfvVLKKDVDA-----------------AY 261
Cdd:pfam12128  647 ALKNA-RLDLRRLFDEK---QSEKDKKNKALAERKDSANERLNSLEAQLK---QLDKKHQAwleeqkeqkreartekqAY 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   262 MIKVE--LEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKsKAEVESWY 339
Cdd:pfam12128  720 WQVVEgaLDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-RQEVLRYF 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   340 QIkvqqLQMSADQHGDSLKTTKNEIS--------ELNRMIQRLRAEIENIKKQSQTLQA---------SVADAEQRGELA 402
Cdd:pfam12128  799 DW----YQETWLQRRPRLATQLSNIEraiselqqQLARLIADTKLRRAKLEMERKASEKqqvrlsenlRGLRCEMSKLAT 874

                          250       260       270
                   ....*....|....*....|....*....|
gi 133778953   403 LK-DAYSKRAELETALQKAKEDLARLLRDY 431
Cdd:pfam12128  875 LKeDANSEQAQGSIGERLAQLEDLKLKRDY 904
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 346-437 1.69e-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: 40.90  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 346 LQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQR------------GELA-----LKDAYS 408
Cdd:COG4942   11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraleQELAaleaeLAELEK 90

                         90       100
                 ....*....|....*....|....*....
gi 133778953 409 KRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG4942   91 EIAELRAELEAQKEELAELLRALYRLGRQ 119
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 264-456 1.74e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  264 KVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKSKAEVE-----SW 338
Cdd:pfam05557   4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkKK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  339 YQIKVQQLQMSADQH----GDSLKTTKNEISELNRMIQR-------LRAEIENIKKQSQTLQASVADAEQRGE------L 401
Cdd:pfam05557  84 YLEALNKKLNEKESQladaREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQnlekqqS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133778953  402 ALKDAYSKRAELETALQK----------AKEDLARL---------LRDYQALMNV----KLALDVEIATYRKLLEGEE 456
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSqeqdseivknSKSELARIpelekelerLREHNKHLNEnienKLLLKEEVEDLKRKLEREE 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
361-450 2.14e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 361 KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELalkdayskrAELETALQKAKEDLARLLRDYQALMNVKLA 440
Cdd:COG4717  431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL---------AELLQELEELKAELRELAEEWAALKLALEL 501

                         90
                 ....*....|
gi 133778953 441 LDVEIATYRK 450
Cdd:COG4717  502 LEEAREEYRE 511
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
267-453 4.19e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 267 LEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLS--MDNNRNLDLDG-------IIAEVRAQYEDiARKSKAEVES 337
Cdd:COG3206  162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEeaklllqQLSELESQLAE-ARAELAEAEA 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 338 WYQIKVQQLQMSADQHGD-----SLKTTKNEISELNRMIQRLRA-------EIENIKKQSQTLQASVADAEQRGELALKD 405
Cdd:COG3206  241 RLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEA 320

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 133778953 406 AY----SKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLE 453
Cdd:COG3206  321 ELealqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 202-443 4.26e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   202 NALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymiKVELEAKmESLKDEINFT 281
Cdd:pfam01576  499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEK-AAAYDKLEKT 574

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   282 RVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAE---VRAQYEDiaRKSKAEVESwYQIKVQQLQMSadQHGDSLK 358
Cdd:pfam01576  575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaISARYAE--ERDRAEAEA-REKETRALSLA--RALEEAL 649

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   359 TTKNEISELNRMiqrLRAEIENIKKQSQTLQASVADAEQrgelalkdaySKRAeLETALQKAKEDLARLLRDYQALMNVK 438
Cdd:pfam01576  650 EAKEELERTNKQ---LRAEMEDLVSSKDDVGKNVHELER----------SKRA-LEQQVEEMKTQLEELEDELQATEDAK 715


                   ....*
gi 133778953   439 LALDV 443
Cdd:pfam01576  716 LRLEV 720
PRK11281 PRK11281
mechanosensitive channel MscK;
318-425 5.05e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  318 AEVRAQYEDIARKSKAEVESwyQIKVQQLQMSADQHgDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADA-- 395
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtr 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 133778953  396 EQRGELALKDAYSKRAELETALQKAKEDLA 425
Cdd:PRK11281  116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLA 145
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
201-434 6.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRT----AAENDFVVLKKdvdaaymIKVELEAKMESLKD 276
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLkelePFYNEYLELKD-------AEKELEREEKELKK 623

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 277 EinftrvlyEAELAQMQTHVSDTsvvlsmdnnrnldlDGIIAEVRAQYEDIARKskaeveswyqikvqqlqMSADQHgds 356
Cdd:PRK03918 624 L--------EEELDKAFEELAET--------------EKRLEELRKELEELEKK-----------------YSEEEY--- 661

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 357 lKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRgelaLKDAYSKRAELETaLQKAKEDLARL---LRDYQA 433
Cdd:PRK03918 662 -EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELEK-LEKALERVEELrekVKKYKA 735


                 .
gi 133778953 434 L 434
Cdd:PRK03918 736 L 736
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 198-450 6.73e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 198 ETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymiKVELEAKMESLKDE 277
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 278 InftRVLYEAELAqmqthVSDTSVVLSMDNnrnldldgiiaevraqYEDIARKskaeveswyqikVQQLQMSADQHGDSL 357
Cdd:COG3883   92 A---RALYRSGGS-----VSYLDVLLGSES----------------FSDFLDR------------LSALSKIADADADLL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 358 KTtkneiselnrmIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNV 437
Cdd:COG3883  136 EE-----------LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204

                        250
                 ....*....|...
gi 133778953 438 KLALDVEIATYRK 450
Cdd:COG3883  205 LAAAEAAAAAAAA 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-446 7.87e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 310 NLD-LDGIIAEVRAQYEDIAR-KSKAEveswyqiKVQQLQMSADQHgdSLKTTKNEISELNRMIQRLRAEIENIKKQSQT 387
Cdd:COG1196  187 NLErLEDILGELERQLEPLERqAEKAE-------RYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEE 257

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 133778953 388 LQASVADAEQRGELALKDAYSKRAELETA---LQKAKEDLARLLRDYQALMNVKLALDVEIA 446
Cdd:COG1196  258 LEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARLEERRRELEERLE 319
 
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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