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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 3.57e-147

Intermediate filament protein;


:

Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 424.33  E-value: 3.57e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGA-EPSRLYSLYEREIRDLRRQLDQLTVERARLQLEIDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953  386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 1.73e-27

Keratin type II head;


:

Pssm-ID: 406589  Cd Length: 160  Bit Score: 107.82  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   14 GFSSGSAIAGGVKRVAFSSG----------SMSGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVG 83
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVscsrsgggggGGGYGAGGGHGGGFGSRSLYNLGGSKSISISVAGGGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   84 GYGAGFGAGGFGGGFGGSFNGRGG---------------------PGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFGGGGfgggggfggggfggggfggggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-458 3.57e-147

Intermediate filament protein;


Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 424.33  E-value: 3.57e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGA-EPSRLYSLYEREIRDLRRQLDQLTVERARLQLEIDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953  386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 1.73e-27

Keratin type II head;


Pssm-ID: 406589  Cd Length: 160  Bit Score: 107.82  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   14 GFSSGSAIAGGVKRVAFSSG----------SMSGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVG 83
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVscsrsgggggGGGYGAGGGHGGGFGSRSLYNLGGSKSISISVAGGGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   84 GYGAGFGAGGFGGGFGGSFNGRGG---------------------PGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFGGGGfgggggfggggfggggfggggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-453 1.58e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.50  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINF 280
Cdd:COG1196   234 LKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  281 trvlYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKSKAEveswyqikvQQLQMSADQHGDSLKTT 360
Cdd:COG1196   314 ----LENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL---------EEKLSALLEELEELFEA 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  361 -KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELA---LKDAYSKRAELETALQKAKEDLARLLRDYQALMN 436
Cdd:COG1196   381 lREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLkeeLKELEAELEELQTELEELNEELEELEEQLEELRD 460
                         250
                  ....*....|....*..
gi 133778953  437 VKLALDVEIATYRKLLE 453
Cdd:COG1196   461 RLKELERELAELQEELQ 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-427 4.50e-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: 4.50e-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
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
220-424 4.52e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 52.61  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 220 SELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymikvelEAKMESLKDEInftrVLYEAELAQMQTHVSDT 299
Cdd:NF033930 157 EELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAE-------EAEIEKLQNEE----VALEAKIAELENQVDNL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 300 SVVLSmDNNRNLDLDGIIAEVRAQYEDIARKSKAEVeSWYQIKVQQLQMSADQHGDSLKTTKNE--ISELNRMIQRLRAE 377
Cdd:NF033930 226 EKELA-EIDESDSEDYIKEGLRAPLESELDAKQAKL-AKKQTELEKLLDSLDPEGKTQDELDKEaaEEELSKKIDELDNE 303
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 133778953 378 IENIKKQSQTLQASVAD-AEQRGELALKDAYSKRAELEtalqKAKEDL 424
Cdd:NF033930 304 VAKLEKEVSDLENSDNNvADYYKEALEKDLATKKAELE----KTQKDL 347
46 PHA02562
endonuclease subunit; Provisional
162-414 3.90e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.24  E-value: 3.90e-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 3.57e-147

Intermediate filament protein;


Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 424.33  E-value: 3.57e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGA-EPSRLYSLYEREIRDLRRQLDQLTVERARLQLEIDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLYEAELAQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  306 DNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQS 385
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778953  386 QTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECR 458
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 1.73e-27

Keratin type II head;


Pssm-ID: 406589  Cd Length: 160  Bit Score: 107.82  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   14 GFSSGSAIAGGVKRVAFSSG----------SMSGGAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVG 83
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVscsrsgggggGGGYGAGGGHGGGFGSRSLYNLGGSKSISISVAGGGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   84 GYGAGFGAGGFGGGFGGSFNGRGG---------------------PGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFGGGGfgggggfggggfggggfggggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-453 1.58e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.50  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINF 280
Cdd:COG1196   234 LKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  281 trvlYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKSKAEveswyqikvQQLQMSADQHGDSLKTT 360
Cdd:COG1196   314 ----LENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL---------EEKLSALLEELEELFEA 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  361 -KNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELA---LKDAYSKRAELETALQKAKEDLARLLRDYQALMN 436
Cdd:COG1196   381 lREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLkeeLKELEAELEELQTELEELNEELEELEEQLEELRD 460
                         250
                  ....*....|....*..
gi 133778953  437 VKLALDVEIATYRKLLE 453
Cdd:COG1196   461 RLKELERELAELQEELQ 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-427 4.50e-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: 4.50e-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
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
220-424 4.52e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 52.61  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 220 SELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymikvelEAKMESLKDEInftrVLYEAELAQMQTHVSDT 299
Cdd:NF033930 157 EELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAE-------EAEIEKLQNEE----VALEAKIAELENQVDNL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 300 SVVLSmDNNRNLDLDGIIAEVRAQYEDIARKSKAEVeSWYQIKVQQLQMSADQHGDSLKTTKNE--ISELNRMIQRLRAE 377
Cdd:NF033930 226 EKELA-EIDESDSEDYIKEGLRAPLESELDAKQAKL-AKKQTELEKLLDSLDPEGKTQDELDKEaaEEELSKKIDELDNE 303
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 133778953 378 IENIKKQSQTLQASVAD-AEQRGELALKDAYSKRAELEtalqKAKEDL 424
Cdd:NF033930 304 VAKLEKEVSDLENSDNNvADYYKEALEKDLATKKAELE----KTQKDL 347
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
188-434 5.31e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 52.41  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  188 TSPKSLDPFFETYINALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVEL 267
Cdd:COG1196   656 SRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQL 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  268 EAKMESLKDEINF---TRVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGI-------IAEVRAQYEDI---ARKSKAE 334
Cdd:COG1196   736 QSRLEELEEELEEleeELEELQERLEELEEELESLEEALAKLKEEIEELEEKrqalqeeLEELEEELEEAerrLDALERE 815
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  335 VESWyQIKVQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQR----------GELALK 404
Cdd:COG1196   816 LESL-EQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDElkeleeekeeLEEELR 894
                         250       260       270
                  ....*....|....*....|....*....|
gi 133778953  405 DAYSKRAELETALQKAKEDLARLLRDYQAL 434
Cdd:COG1196   895 ELESELAELKEEIEKLRERLEELEAKLERL 924
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-450 7.28e-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: 7.28e-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 2.95e-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: 2.95e-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 3.90e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 49.24  E-value: 3.90e-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 1.29e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.97  E-value: 1.29e-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
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
265-461 5.55e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.86  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  265 VELEAKMESLKDEINFTrvlyEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIARKSKAEVESWYQI--K 342
Cdd:COG1196   670 KELEEELAELEAQLEKL----EEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELeeE 745
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  343 VQQLQMSADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQ---RGELALKDAYSKRAELETALQK 419
Cdd:COG1196   746 LEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEeleEAERRLDALERELESLEQRRER 825
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 133778953  420 AKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEECRMSG 461
Cdd:COG1196   826 LEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEE 867
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-459 5.84e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.86  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  201 INALRKNLDTLSNDKGRLQSELKMMQDSVEDFKtKYEEEINKRTAAENDFVVLKKDvdaaymikvELEAKMESLKDEINf 280
Cdd:COG1196   181 LERTEENLERLEDLLEELEKQLEKLERQAEKAE-RYQELKAELRELELALLLAKLK---------ELRKELEELEEELS- 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  281 trvLYEAELAQMQTHVSDTSVvlsmdnnrnldldgIIAEVRAQYEDIARKSKAEVESWYQIK---------VQQLQMSAD 351
Cdd:COG1196   250 ---RLEEELEELQEELEEAEK--------------EIEELKSELEELREELEELQEELLELKeeieelegeISLLRERLE 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  352 QHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDLARLLRDY 431
Cdd:COG1196   313 ELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAEL 392
                         250       260
                  ....*....|....*....|....*...
gi 133778953  432 QALMNVKLALDVEIATYRKLLEGEECRM 459
Cdd:COG1196   393 AEIRNELEELKREIESLEERLERLSERL 420
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-453 3.00e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  201 INALRKNLDTLSNDK------GRLQSELKMMQDSVedFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESL 274
Cdd:COG1196   195 LEELEKQLEKLERQAekaeryQELKAELRELELAL--LLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEEL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  275 KDEINFTRVLYEaELAQMQTHVSDTSVVLSMDNNRNLD--LDGIIAEVRAQYEDIARKSKAEVESWYQIKVQQLQMSADQ 352
Cdd:COG1196   273 KSELEELREELE-ELQEELLELKEEIEELEGEISLLRErlEELENELEELEERLEELKEKIEALKEELEERETLLEELEQ 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  353 hgdSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVadaeqRGELALKDAysKRAELETALQKAKEDLARLLRDYQ 432
Cdd:COG1196   352 ---LLAELEEAKEELEEKLSALLEELEELFEALREELAEL-----EAELAEIRN--ELEELKREIESLEERLERLSERLE 421
                         250       260
                  ....*....|....*....|.
gi 133778953  433 ALMNVKLALDVEIATYRKLLE 453
Cdd:COG1196   422 DLKEELKELEAELEELQTELE 442
PRK09039 PRK09039
peptidoglycan -binding protein;
286-426 3.23e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.03  E-value: 3.23e-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
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
138-409 3.62e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  138 EIQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPKSLDpfFETYINALRKNLDTLSNDKGR 217
Cdd:COG1196   748 ELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEE--AERRLDALERELESLEQRRER 825
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  218 LQSELKMMQDSVEDfktkYEEEINkrtAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFTRVLY----------EA 287
Cdd:COG1196   826 LEQEIEELEEEIEE----LEEKLD---ELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKeeleeelrelES 898
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953  288 ELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEDIarkSKAEVESWYQIKVQQLQMSADQHGDSLKTTKNEISEL 367
Cdd:COG1196   899 ELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEE---YEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEV 975
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 133778953  368 NRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSK 409
Cdd:COG1196   976 EERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKETFDK 1017
PRK01156 PRK01156
chromosome segregation protein; Provisional
138-427 5.16e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.97  E-value: 5.16e-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 5.54e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 318193 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 5.54e-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 8.22e-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: 8.22e-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 1.01e-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: 1.01e-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
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
264-456 1.65e-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: 368498 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 1.65e-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
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
332-456 2.31e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 39.66  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 332 KAEVESWYQIKVQQLQMS-----ADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQR---GELAL 403
Cdd:COG1579    3 NNNLKSLLAIQKLDLEKDrleprIKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERikrAEEKL 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 133778953 404 KDAYSKRA--ELETALQKAKEDLARLLRDYQALMNVKLALDVEIATYRKLLEGEE 456
Cdd:COG1579   83 SAVKDERElrALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLE 137
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
202-443 3.23e-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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   202 NALRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymiKVELEAKmESLKDEINFT 281
Cdd:pfam01576  499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEAL---TQRLEEK-AAAYDKLEKT 574
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   282 RVLYEAELAQMQTHVSDTSVVLSMDNNRNLDLDGIIAE---VRAQYEDiaRKSKAEVESwYQIKVQQLQMSAdqhgdSLK 358
Cdd:pfam01576  575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaISARYAE--ERDRAEAEA-REKETRALSLSR-----ALE 646
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953   359 TTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQrgelalkdaySKRAeLETALQKAKEDLARLLRDYQALMNVK 438
Cdd:pfam01576  647 EALEAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELER----------SKRA-LEQQVEEMKTQLEELEDELQATEDAK 715

                   ....*
gi 133778953   439 LALDV 443
Cdd:pfam01576  716 LRLEV 720
PRK11281 PRK11281
mechanosensitive channel MscK;
318-425 4.78e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 4.78e-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 6.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.03e-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
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
269-438 7.25e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 38.12  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 269 AKMESLKDEINFTRVLYEAELAQMQTHVSDtsvvlsmdnnrnLDLDgiIAEVRAQYEDIARKSKAEVEswyQIKVQQLQM 348
Cdd:COG1579   34 KKAKAELEALNKALEALEIELEDLENQVSQ------------LESE--IQEIRERIKRAEEKLSAVKD---ERELRALNI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 349 SADQHGDSLKTTKNEISELNRMIQRLRAEIENIKKQSQTLQASVADAEQRGELALKDAYSKRAELETALQKAKEDL-ARL 427
Cdd:COG1579   97 EIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELKEKLdPEL 176
                        170
                 ....*....|.
gi 133778953 428 LRDYQALMNVK 438
Cdd:COG1579  177 LSEYERIRKNK 187
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
172-428 7.56e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 38.90  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 172 KVLETKWNLLQQQTTTTSPKSldpffetYINAlRKNLDTLSNDKGRLQSELKMMQDSVEDFKTKYEEEINKRTAAENDFV 251
Cdd:COG4477  171 KKLENIEEELSQFVELTSSGD-------YIEA-REVLEEAEEHMIALRSIMERIPSLLAELQTELPGQLQDLKAGYRDMK 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 252 VlkkdvDAAYMIKVELEAKMESLKDEINFTRVLY--------EAELAQMQTHVSDT-----------SVVLSMDNNRNLD 312
Cdd:COG4477  243 E-----EGYHLEHVNIDSRLERLKEQLVENSELLtqleldeaEEELGLIQEKIESLydllereveakNVVEENLPILPDY 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778953 313 LDGIIAEVRAQYEDIARKSK----AEVESWYQIKVQQLQMSADQHGDSL--KTTKNEI--SELNRMIQRLRAEIENIKKQ 384
Cdd:COG4477  318 LEKAKENNEHLKEEIERVKEsyrlAETELGSVRKFEKELKELESVLDEIleNIEAQEVaySELQDNLEEIEKALTDIEDE 397
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 133778953 385 SQTLQASVADAEqrgelalKDAYSKRAELETaLQKAKEDLARLL 428
Cdd:COG4477  398 QEKVQEHLTSLR-------KDELEARENLER-LKSKLHEIKRYM 433
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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