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Conserved domains on  [gi|301612553|ref|XP_002935776|]
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keratin, type II cytoskeletal-like [Xenopus tropicalis]

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;
158-474 5.00e-136

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 397.75  E-value: 5.00e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  158 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQggqvKGSRKNNIDPIFDAYINSLKRQLDALQNDKLRLDGE 237
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK----KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  238 LRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRTFFEAELGELQAQISDTSV 317
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  318 VLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENV 397
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301612553  398 KKQIAKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEEFR 474
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
127-155 4.65e-13

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 66.99  E-value: 4.65e-13
                          10        20
                  ....*....|....*....|....*....
gi 301612553  127 PSVGIQEVTVNQSLLAPLNLEIDPTIQKV 155
Cdd:pfam16208 128 PPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
158-474 5.00e-136

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 397.75  E-value: 5.00e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  158 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQggqvKGSRKNNIDPIFDAYINSLKRQLDALQNDKLRLDGE 237
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK----KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  238 LRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRTFFEAELGELQAQISDTSV 317
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  318 VLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENV 397
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301612553  398 KKQIAKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEEFR 474
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
127-155 4.65e-13

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 66.99  E-value: 4.65e-13
                          10        20
                  ....*....|....*....|....*....
gi 301612553  127 PSVGIQEVTVNQSLLAPLNLEIDPTIQKV 155
Cdd:pfam16208 128 PPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-450 8.64e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 8.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   155 VRLEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGGQVkgsrknnidpifDAYINSLKRQLDALQNDKLRL 234
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL------------RKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   235 DGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRTffeaELGELQAQISD 314
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE----ALDELRAELTL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   315 TSVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVyqgkvQELQAsageqgdvlrntksEISELNRKSQRLKAEI 394
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-----ESLAA--------------EIEELEELIEELESEL 875

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 301612553   395 ENVKKQIAKLQASITEAEERGDLV---LKDAQSKLAELEAALQKVKQDMARQLREYQEL 450
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
PRK09039 PRK09039
peptidoglycan -binding protein;
287-446 6.08e-08

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 54.97  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 287 VDALTDEL---NFLRTFF--------------EAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDI-AKKSR 348
Cdd:PRK09039  20 VDALSTLLlviMFLLTVFvvaqfflsreisgkDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 349 AEA-ESVYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGdlvlKDAQSKLA 427
Cdd:PRK09039 100 LQAlLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIA 175

                        170       180       190
                 ....*....|....*....|....*....|.
gi 301612553 428 ----ELEAAL-QKVkQDMAR-------QLRE 446
Cdd:PRK09039 176 dlgrRLNVALaQRV-QELNRyrseffgRLRE 205
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 302-472 1.36e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 302 EAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAeaesvYQGKVQELQASAGEQGDVLRNTKSEIS 381
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-----AQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 382 ELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDL---VLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALD 458
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170
                 ....*....|....
gi 301612553 459 VEIATYRKLLEGEE 472
Cdd:COG1196  393 RAAAELAAQLEELE 406
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
158-474 5.00e-136

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 397.75  E-value: 5.00e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  158 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQggqvKGSRKNNIDPIFDAYINSLKRQLDALQNDKLRLDGE 237
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK----KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  238 LRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRTFFEAELGELQAQISDTSV 317
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  318 VLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENV 397
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301612553  398 KKQIAKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEEFR 474
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
127-155 4.65e-13

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 66.99  E-value: 4.65e-13
                          10        20
                  ....*....|....*....|....*....
gi 301612553  127 PSVGIQEVTVNQSLLAPLNLEIDPTIQKV 155
Cdd:pfam16208 128 PPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 155-450 8.64e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 8.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   155 VRLEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGGQVkgsrknnidpifDAYINSLKRQLDALQNDKLRL 234
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL------------RKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   235 DGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRTffeaELGELQAQISD 314
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE----ALDELRAELTL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   315 TSVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVyqgkvQELQAsageqgdvlrntksEISELNRKSQRLKAEI 394
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-----ESLAA--------------EIEELEELIEELESEL 875

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 301612553   395 ENVKKQIAKLQASITEAEERGDLV---LKDAQSKLAELEAALQKVKQDMARQLREYQEL 450
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
PRK09039 PRK09039
peptidoglycan -binding protein;
287-446 6.08e-08

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 54.97  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 287 VDALTDEL---NFLRTFF--------------EAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDI-AKKSR 348
Cdd:PRK09039  20 VDALSTLLlviMFLLTVFvvaqfflsreisgkDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 349 AEA-ESVYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGdlvlKDAQSKLA 427
Cdd:PRK09039 100 LQAlLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIA 175

                        170       180       190
                 ....*....|....*....|....*....|.
gi 301612553 428 ----ELEAAL-QKVkQDMAR-------QLRE 446
Cdd:PRK09039 176 dlgrRLNVALaQRV-QELNRyrseffgRLRE 205
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 198-450 1.78e-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: 54.30  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   198 GGQVKGSRKNNIDPIFDAYINSLKRQLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAY 277
Cdd:TIGR02169  657 GGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   278 MGKVELEAKVDALTDELNFLRTF---FEAELGELQAQISdtSVVLSMDNNRALDLESIIAEVKSQYEDIaKKSRAEAESV 354
Cdd:TIGR02169  737 ERLEELEEDLSSLEQEIENVKSElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKL-EEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   355 YQGKVQELQASAGEQG---DVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERgdlvLKDAQSKLAELEA 431
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEyleKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA----LRDLESRLGDLKK 889

                          250
                   ....*....|....*....
gi 301612553   432 ALQKVKQDMARQLREYQEL 450
Cdd:TIGR02169  890 ERDELEAQLRELERKIEEL 908
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 212-476 2.83e-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: 53.53  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   212 IFDAYINSLKRQLDALQ---NDKLRLDGELRNMQDLvddfknKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVD 288
Cdd:TIGR02169  188 RLDLIIDEKRQQLERLRrerEKAERYQALLKEKREY------EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   289 ALTDELNFLrtffEAELGELQAQISDtsvvlsMDNNRALDLESIIAEVKSQyedIAKKSRAEAEsvyqgKVQELQASAGE 368
Cdd:TIGR02169  262 ELEKRLEEI----EQLLEELNKKIKD------LGEEEQLRVKEKIGELEAE---IASLERSIAE-----KERELEDAEER 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   369 QgdvlRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLVLKDAQS----------KLAELEAALQKVKQ 438
Cdd:TIGR02169  324 L----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaetrdELKDYREKLEKLKR 399

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 301612553   439 DMARQLREYQELMNVKLALDVEIATYRKLLEGEEFRLN 476
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-481 3.03e-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: 53.52  E-value: 3.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   307 ELQAQISDTSVVLSMDNNRALD-----LESIIAEVKSQYEDIAKKSRAEAESVYQ--GKVQELQASAGEQGDVLRNTKSE 379
Cdd:TIGR02168  217 ELKAELRELELALLVLRLEELReeleeLQEELKEAEEELEELTAELQELEEKLEElrLEVSELEEEIEELQKELYALANE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   380 ISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLV---LKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLA 456
Cdd:TIGR02168  297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376

                          170       180
                   ....*....|....*....|....*...
gi 301612553   457 LDVEIATYRK---LLEGEEFRLNSDVNN 481
Cdd:TIGR02168  377 LEEQLETLRSkvaQLELQIASLNNEIER 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-477 8.92e-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: 8.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   217 INSLKRQLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNF 296
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   297 LrtffEAELGELQAQISDtsvvlsmDNNRALDLESIIAEVKSQYEDIAKKSRAEAESV--YQGKVQELQASAGEQGDVLR 374
Cdd:TIGR02168  314 L----ERQLEELEAQLEE-------LESKLDELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   375 NTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLVLKDAQS-KLAELEAALQKVKQDMARQLREYQELMNV 453
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEA 462

                          250       260
                   ....*....|....*....|....
gi 301612553   454 KLALDVEIATYRKLLEGEEFRLNS 477
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQ 486
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 302-472 1.36e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 302 EAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAeaesvYQGKVQELQASAGEQGDVLRNTKSEIS 381
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-----AQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 382 ELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDL---VLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALD 458
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170
                 ....*....|....
gi 301612553 459 VEIATYRKLLEGEE 472
Cdd:COG1196  393 RAAAELAAQLEELE 406
PRK01156 PRK01156
chromosome segregation protein; Provisional
 147-472 3.20e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 50.29  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 147 EIDPTIQKVRLEE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQG-----GQVKGSRK-NNIDPIFDAYINS 219
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcGTTLGEEKsNHIINHYNEKKSR 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 220 LKRQLDALQNDKLRLDGELRNMQDLVDDFK----NKYEDEINKRTSAENEFVVIKKDVDAAymgkVELEAKVDALTDELN 295
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIKIKINEL----KDKHDKYEEIKNRYK 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 296 FLrtffeaELGELQAQISDTSVVLSMDNNRALD-LESIIAEVKSQYEDIAKKSRaEAESVYQGKVQELQASAGEQGD--- 371
Cdd:PRK01156 557 SL------KLEDLDSKRTSWLNALAVISLIDIEtNRSRSNEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENean 629

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 372 VLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQaSITEAEERGDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELM 451
Cdd:PRK01156 630 NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILR 708

                        330       340
                 ....*....|....*....|.
gi 301612553 452 NVKLALDVEIATYRKLLEGEE 472
Cdd:PRK01156 709 TRINELSDRINDINETLESMK 729
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 347-448 3.51e-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: 49.38  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 347 SRAEAESVYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERgdlvLKDAQSKL 426
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEI 92

                         90       100
                 ....*....|....*....|..
gi 301612553 427 AELEAALQKVKQDMARQLREYQ 448
Cdd:COG4942   93 AELRAELEAQKEELAELLRALY 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 282-469 6.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 6.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 282 ELEAKVDALTDELNFLrtffEAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAEsvyqgKVQE 361
Cdd:COG1196  243 ELEAELEELEAELEEL----EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-----RRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 362 LQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERgdlvLKDAQSKLAELEAALQKVKQDMA 441
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELL 389

                        170       180
                 ....*....|....*....|....*...
gi 301612553 442 RQLREYQELMNVKLALDVEIATYRKLLE 469
Cdd:COG1196  390 EALRAAAELAAQLEELEEAEEALLERLE 417
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 223-473 8.08e-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: 48.22  E-value: 8.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 223 QLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRtffe 302
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR---- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 303 AELGELQAQISDTSVVLSMdNNRALDLESIIAEvksqyEDIAKKSRAEAesVYQGKVQELQasagEQGDVLRNTKSEIse 382
Cdd:COG4942   97 AELEAQKEELAELLRALYR-LGRQPPLALLLSP-----EDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAEL-- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 383 lnrksQRLKAEIENVKKQIAKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIA 462
Cdd:COG4942  163 -----AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237

                        250
                 ....*....|.
gi 301612553 463 TYRKLLEGEEF 473
Cdd:COG4942  238 AAAERTPAAGF 248
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
284-481 1.19e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  284 EAKVDALTDELNFLrtffEAELGELQAQISDTSVVLSMDNNRALDLESIiAEVKSQYEDIAkksraEAESVYQGKVQELQ 363
Cdd:COG4913   609 RAKLAALEAELAEL----EEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVA-----SAEREIAELEAELE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  364 AsageqgdvLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERgdlvLKDAQSKLAELEAALQKVKQDMARQ 443
Cdd:COG4913   679 R--------LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLARLE 746

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 301612553  444 LREYQELMNVKLALDVEIATYRKLLEGEEFRLNSDVNN 481
Cdd:COG4913   747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNR 784
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
283-487 1.77e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 283 LEAKVDALTDELNFLRTFFEAELGELQAQISDTSVVLS---------MDNNRALDLESIIAEVKSQYEDiAKKSRAEAES 353
Cdd:COG3206  162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAE-ARAELAEAEA 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 354 VYQGKVQELQASAGEQGDVLRNT------------KSEISELNRKS-------QRLKAEIENVKKQIAKLQASITEAEER 414
Cdd:COG3206  241 RLAALRAQLGSGPDALPELLQSPviqqlraqlaelEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEA 320

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301612553 415 gdlVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLEG-EEFRLNSDVNNVSISVI 487
Cdd:COG3206  321 ---ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEALTVGNVRVI 391
46 PHA02562
endonuclease subunit; Provisional
 175-444 3.21e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.55  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 175 DKVRFLEQQNKVLETKWSLLQEQggqvkgsrknnIDpIFDAYINSLKRQLDALQNDKlrldgelrnmQDLVDDFKNKYED 254
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-----------IK-TYNKNIEEQRKKNGENIARK----------QNKYDELVEEAKT 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 255 ---EINKRTSAENEFVVIKKDVDAAY----MGKVELEAKVDALTDELNFLRtffeaELGELQA---QISDTsvvlsmdNN 324
Cdd:PHA02562 232 ikaEIEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE-----KGGVCPTctqQISEG-------PD 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 325 RALDLESIIAEVKSQYEDIAKKsraeaesvyQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKL 404
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTA---------IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 301612553 405 QAS-ITEAEERGDLV--LKDAQSKLAELEaaLQKVKQDMARQL 444
Cdd:PHA02562 371 QAEfVDNAEELAKLQdeLDKIVKTKSELV--KEKYHRGIVTDL 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-475 3.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 329 LESIIAEVKSQYEDIAKKSRAeAES--VYQGKVQELQASAG-----EQGDVLRNTKSEISELNRKSQRLKAEIENVKKQI 401
Cdd:COG1196  191 LEDILGELERQLEPLERQAEK-AERyrELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAEL 269

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301612553 402 AKLQASITEAEERgdlvLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEEFRL 475
Cdd:COG1196  270 EELRLELEELELE----LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-469 5.38e-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: 46.20  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   237 ELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLrtffEAELGELQAQISDTS 316
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL----EAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   317 vvlsmdnnraLDLESIIAEVKSQYEDIAKKSRAEAESvyQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEI-- 394
Cdd:TIGR02168  754 ----------KELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAan 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   395 -----ENVKKQIAKLQASITEAEERgdlvLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLE 469
Cdd:TIGR02168  822 lrerlESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 194-438 1.00e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   194 LQEQGGQVKGSRKNnidpiFDAYINSLKRQLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDV 273
Cdd:TIGR02169  292 VKEKIGELEAEIAS-----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   274 DAAYMGKVELEAKVDALTDELNFLRTffeaELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDIakksraeaes 353
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI---------- 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   354 vyQGKVQELQASAGEQGDvlrntksEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERgdlvLKDAQSKLAELEAAL 433
Cdd:TIGR02169  433 --EAKINELEEEKEDKAL-------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE----LSKLQRELAEAEAQA 499


                   ....*
gi 301612553   434 QKVKQ 438
Cdd:TIGR02169  500 RASEE 504
PRK11281 PRK11281
mechanosensitive channel MscK;
334-441 1.66e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  334 AEVKSQYEDIAKKSRAEAESvyQGKVQELQASAgEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEA-- 411
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTL-ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtr 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 301612553  412 EERGDLVLKDAQSKLAELEAALQKVKQDMA 441
Cdd:PRK11281  116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLA 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-453 3.75e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   147 EIDPTIQKVRLEE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGGQVKgSRKNNIDPIFDAY--------- 216
Cdd:TIGR02168  224 ELELALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKELYALaneisrleq 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   217 -INSLKRQLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELN 295
Cdd:TIGR02168  303 qKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   296 FLRtffeAELGELQAQISDTsvvlsmdNNRALDLESIIAEVKSQYEDIAKKSRAEAESVYQGKVQELQASAGEQGDVLRN 375
Cdd:TIGR02168  383 TLR----SKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   376 TKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLV--LKDAQSKLAELEAALQKVKQDMARQLREYQELMNV 453
Cdd:TIGR02168  452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 261-466 5.39e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 5.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 261 SAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLrtffEAELGELQAQISDTSVvlSMDNNRAlDLESIIAEVKSQY 340
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEERR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 341 EDIAKKSRAEAESVYQGKVQELQASAGEQGDVLRNTK--SEISELNRKS----QRLKAEIENVKKQIAKLQASITEAEER 414
Cdd:COG3883   86 EELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSalSKIADADADLleelKADKAELEAKKAELEAKLAELEALKAE 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 301612553 415 GDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRK 466
Cdd:COG3883  166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
217-446 5.65e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 217 INSLKRQLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTsaenEFVVIKKDVDAAYMGKVELEAKVDALTDELNF 296
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAEIEDLRETIAETEREREELAEEVRD 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 297 LRtffeAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDI----------AKKSRAEAESV------YQGKVQ 360
Cdd:PRK02224 284 LR----ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELrdrleecrvaAQAHNEEAESLredaddLEERAE 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 361 ELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLVLK---DAQSKLAELEAALQKVK 437
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTAR 439

                        250
                 ....*....|.
gi 301612553 438 QDM--ARQLRE 446
Cdd:PRK02224 440 ERVeeAEALLE 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
325-466 6.20e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  325 RALDLESIIAEVKSQYEDI-AKKSRAEAE-SVYQGKVQELQAS-AGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQI 401
Cdd:COG4913   289 RLELLEAELEELRAELARLeAELERLEARlDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301612553  402 AKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRK 466
Cdd:COG4913   369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 325-472 6.42e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 325 RALDLESIIAEVKSQYEDIAKKSRAEAEsvYQGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKL 404
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEE--LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301612553 405 QASITEAEERgdlvLKDAQSKLAELEAALQKVKQDMARQLREYQELMNVKLALDVEIATYRKLLEGEE 472
Cdd:COG1196  308 EERRRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
282-445 8.53e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 41.76  E-value: 8.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 282 ELEAKVDALTDEL--NFLRtFFEAELGELQAQISDTSV-VLSMDN-NRALDLEsiiAEVKSQYEDIAKksraeaesvYQG 357
Cdd:COG3524  162 ESEELVNQLSERAreDAVR-FAEEEVERAEERLRDAREaLLAFRNrNGILDPE---ATAEALLQLIAT---------LEG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 358 KVQELQASageqgdvLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLVLKDAQSKLAELE------- 430
Cdd:COG3524  229 QLAELEAE-------LAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLLAEYERLELErefaeka 301

                        170       180
                 ....*....|....*....|
gi 301612553 431 -----AALQKVKQDMARQLR 445
Cdd:COG3524  302 ytsalAALEQARIEAARQQR 321
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-422 1.08e-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: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   158 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGGQVKGSRKNNIDPIFDA--YINSLKRQLDALQNDKLRLD 235
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATerRLEDLEEQIEELSEDIESLA 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   236 GELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDAAYMGKVELEAKVDALTDELNFLRTffeaELGELQAQISDT 315
Cdd:TIGR02168  859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE----KLAQLELRLEGL 934

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   316 SVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAEsvyqGKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIE 395
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE 1010

                          250       260
                   ....*....|....*....|....*..
gi 301612553   396 NVKKQIAKLQASITEAEERGDLVLKDA 422
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEIDREARERFKDT 1037
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 245-425 1.15e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.84  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 245 VDDFKNKYEDEINKRTSAENEfvvikkdvdaaymgkveLEAKVDALTDELNFLRTF--FEAELGELQAQISDTSVVLSMD 322
Cdd:PRK05771  91 VEEELEKIEKEIKELEEEISE-----------------LENEIKELEQEIERLEPWgnFDLDLSLLLGFKYVSVFVGTVP 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 323 NNRALDLESIIAEVKSQYED-----------IAKKSRAEAESVYQG-KVQELQASA-GEQGDVLRNTKSEISELNRKSQR 389
Cdd:PRK05771 154 EDKLEELKLESDVENVEYIStdkgyvyvvvvVLKELSDEVEEELKKlGFERLELEEeGTPSELIREIKEELEEIEKERES 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 301612553 390 LKAEIENVKKQIAKLQASITEA----EERGDLVLKDAQSK 425
Cdd:PRK05771 234 LLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTD 273
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 285-439 1.22e-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: 40.68  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 285 AKVDALTDELNFLRTFFEAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDI-AKKSRAEAESVYQGKVQELQ 363
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVeARIKKYEEQLGNVRNNKEYE 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301612553 364 ASAGEqgdvLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQD 439
Cdd:COG1579   93 ALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 151-414 1.72e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  151 TIQKVRLEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGGQVKGSRKNNIDPI--FDAYINSLKRQLDALQ 228
Cdd:TIGR04523  58 NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKnkLEVELNKLEKQKKENK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  229 NDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDvdaaymgKVELEAKVDALTDELNFLRTF-------- 300
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNKLLKLELLlsnlkkki 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  301 -----FEAELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDIaKKSRAEAESVYQGKVQELQASAG---EQGDV 372
Cdd:TIGR04523 211 qknksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL-KDEQNKIKKQLSEKQKELEQNNKkikELEKQ 289

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 301612553  373 LRNTKSEISELNRKSQ-----RLKAEIENVKKQIAKLQASITEAEER 414
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKI 336
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 316-475 1.88e-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: 41.20  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   316 SVVLSMDNNRAlDLESIIAEVKSQYEDIaKKSRAEAESvyqgKVQELQASAGEQGDVLRNTKSEISELNRKSQRLKAEIE 395
Cdd:TIGR02168  670 SSILERRREIE-ELEEKIEELEEKIAEL-EKALAELRK----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   396 NVKKQIAKLQASITEAEERGDLVLKD---AQSKLAELEAALQKVKQDMARQL-------REYQELMNVKLALDVEIATYR 465
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERleeAEEELAEAEAEIEELEAQIEQLKeelkalrEALDELRAELTLLNEEAANLR 823

                          170
                   ....*....|
gi 301612553   466 KLLEGEEFRL 475
Cdd:TIGR02168  824 ERLESLERRI 833
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 214-438 1.94e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 214 DAYINSLKRQLDALQNDKLRLDGELRNMQDLVDDFKNKYEDEINKRTSAENEFVVIKKDVDaaymgkvELEAKVDALTDE 293
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 294 L-NFLRTFFEAelgelQAQISDTSVVLSMDNnraldlesiIAEVKSQYEDIAKKSRAEAESVyqGKVQELQASAGEQGDV 372
Cdd:COG3883   88 LgERARALYRS-----GGSVSYLDVLLGSES---------FSDFLDRLSALSKIADADADLL--EELKADKAELEAKKAE 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301612553 373 LRNTKSEISELNRKSQRLKAEIEnvkKQIAKLQASITEAEERGDLVLKDAQSKLAELEAALQKVKQ 438
Cdd:COG3883  152 LEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 282-469 2.27e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   282 ELEAKVDALTDELNFLRtffeAELGELQAQISDTSVVLSmdnnralDLESIIAEVKSQYEDIAKKSRAEAEsvyqgKVQE 361
Cdd:TIGR02169  678 RLRERLEGLKRELSSLQ----SELRRIENRLDELSQELS-------DASRKIGEIEKEIEQLEQEEEKLKE-----RLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   362 LQASAGEQGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQAS--------ITEAEERGDLVLKDAQSKLAELEAAL 433
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsripeIQAELSKLEEEVSRIEARLREIEQKL 821

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 301612553   434 QKVKQDMARQLREYQELMNVKLALDVEIATYRKLLE 469
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 378-475 2.35e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553 378 SEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERgdlvLKDAQSKLAELEAALQKVKQDMARqlreYQE-LMNVK-- 454
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKK----YEEqLGNVRnn 88

                         90       100
                 ....*....|....*....|....
gi 301612553 455 ---LALDVEIATYRKLLEGEEFRL 475
Cdd:COG1579   89 keyEALQKEIESLKRRISDLEDEI 112
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 374-435 4.06e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 40.15  E-value: 4.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301612553 374 RNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEER-GDLVLKDaQSKLAELEAALQK 435
Cdd:PRK10636 545 KDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKlGDSELYD-QSRKAELTACLQQ 606
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 251-473 4.88e-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: 39.82  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   251 KYEDEINKRTSAENEFVVIKKDVDAAYM-----------GKVELEAKVDALTDELNFLRTFFEAELGELQAQISDTSVVL 319
Cdd:pfam12128  245 KLQQEFNTLESAELRLSHLHFGYKSDETliasrqeerqeTSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSEL 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553   320 SMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVYqgkvQELQASAGEQGDVLRNTKSEISelnRKSQRLKAEIENVKK 399
Cdd:pfam12128  325 EALEDQHGAFLDADIETAAADQEQLPSWQSELENLE----ERLKALTGKHQDVTAKYNRRRS---KIKEQNNRDIAGIKD 397

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301612553   400 QIAKlqasITEAEERGDLVLKDAqskLAELEAALQKVKQDMARQLREYQELM-----NVKLALDVEIATYRKLLEGEEF 473
Cdd:pfam12128  398 KLAK----IREARDRQLAVAEDD---LQALESELREQLEAGKLEFNEEEYRLksrlgELKLRLNQATATPELLLQLENF 469
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 158-450 6.34e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  158 EEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGGQVKGSRKNNIDPIF---------DAYINSLKRQLDALQ 228
Cdd:TIGR04523  93 KNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKkkekeleklNNKYNDLKKQKEELE 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  229 NDKLRLDGELRNMQDLVDDFKNKY--------------------EDEINKrtsAENEFVVIKKDVDAAYMGKVELEAKVD 288
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkkiqknkslESQISE---LKKQNNQLKDNIEKKQQEINEKTTEIS 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  289 ALTDELNFLRTffeaELGELQAQISDTSVVLSMDNNRALDLESIIAEVKSQYEDIAKKSRAEAESVYQGKVQELQASAGE 368
Cdd:TIGR04523 250 NTQTQLNQLKD----EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301612553  369 QGDVLRNTKSEISELNRKSQRLKAEIENVKKQIAKLQASITEAEERGDLVLKDAQSKLAELEaALQKVKQDMARQLREYQ 448
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQE 404


                  ..
gi 301612553  449 EL 450
Cdd:TIGR04523 405 KL 406
 
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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