NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1940128062|ref|NP_001008806|]
View 

keratin, type II cytoskeletal 4 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-456 1.36e-147

Intermediate filament protein;


:

Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 425.49  E-value: 1.36e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPRNLDPFFETYINALRKNLDTLSNDKGRLQSELKLM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGA-EPSRLYSLYEREIRDLRRQLDQLTVERARLQLEIDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 306 DNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQ- 384
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQk 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940128062 385 -TLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 456
Cdd:pfam00038 241 aSLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 4.15e-34

Keratin type II head;


:

Pssm-ID: 406589  Cd Length: 160  Bit Score: 126.31  E-value: 4.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  14 GFSSGSAVAGGVKRVAFSSASMSG----------GAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVG 83
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSCSRsggggggggyGAGGGHGGGFGSRSLYNLGGSKSISISVAGGGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  84 GYGAGFGAGGFGGGFGGSFNGRGG---------------------PGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFGGGGfgggggfggggfggggfggggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-456 1.36e-147

Intermediate filament protein;


Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 425.49  E-value: 1.36e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPRNLDPFFETYINALRKNLDTLSNDKGRLQSELKLM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGA-EPSRLYSLYEREIRDLRRQLDQLTVERARLQLEIDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 306 DNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQ- 384
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQk 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940128062 385 -TLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 456
Cdd:pfam00038 241 aSLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 4.15e-34

Keratin type II head;


Pssm-ID: 406589  Cd Length: 160  Bit Score: 126.31  E-value: 4.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  14 GFSSGSAVAGGVKRVAFSSASMSG----------GAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVG 83
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSCSRsggggggggyGAGGGHGGGFGSRSLYNLGGSKSISISVAGGGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  84 GYGAGFGAGGFGGGFGGSFNGRGG---------------------PGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFGGGGfgggggfggggfggggfggggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
146-453 3.34e-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: 56.60  E-value: 3.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  146 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPRNLDpfFETYINALRKNLDTLSNDKGRLQSELKL 224
Cdd:TIGR02168  674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  225 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDvdaaymiKVELEAKMESLKDEINfmrvLYEAELSQMQTHVSDTSVVLS 304
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  305 MDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQ--QLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENik 382
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEE-- 898
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062  383 kqtLQASVADAE-QRGEL--ALKDAYTKRADLETALQKAKEDLA----RLMRDYQELMNVKLALDVEIATYRKLLEGE 453
Cdd:TIGR02168  899 ---LSEELRELEsKRSELrrELEELREKLAQLELRLEGLEVRIDnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRR 973
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-451 7.97e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.11  E-value: 7.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  201 INALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINF 280
Cdd:COG1196    234 LKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  281 mrvlYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEveswyqikvQQLQMSADQHGDSLKST 360
Cdd:COG1196    314 ----LENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL---------EEKLSALLEELEELFEA 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  361 -KNEISELNRMIQRIRSEIENIKKQT--LQASVADAEQRGELA---LKDAYTKRADLETALQKAKEDLARLMRDYQELMN 434
Cdd:COG1196    381 lREELAELEAELAEIRNELEELKREIesLEERLERLSERLEDLkeeLKELEAELEELQTELEELNEELEELEEQLEELRD 460
                          250
                   ....*....|....*..
gi 1940128062  435 VKLALDVEIATYRKLLE 451
Cdd:COG1196    461 RLKELERELAELQEELQ 477
PRK01156 PRK01156
chromosome segregation protein; Provisional
134-454 2.16e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 50.67  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 134 EIDPEIQKIRTAE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTT---------TTSPRNLDPFFETYINA 203
Cdd:PRK01156  401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgEEKSNHIINHYNEKKSR 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 204 LRKNLDTLSNDKGRLQSE---LKLMQDSVEDFKT-KYEEEINKRTAAENDfvvLKKDVDAAYMIKvELEAKMESLKDEIN 279
Cdd:PRK01156  481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEInKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 280 FMRVlyeAELSQMQTHVSDTSVVLSmdnnrNLDLDGIiaevRAQYEEIARKSKAEVESWYQIKVQQLQMSA--------- 350
Cdd:PRK01156  557 SLKL---EDLDSKRTSWLNALAVIS-----LIDIETN----RSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksirei 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 351 DQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQTLQA-SVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDY 429
Cdd:PRK01156  625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
                         330       340
                  ....*....|....*....|....*
gi 1940128062 430 QELMNVKLALDVEIATYRKLLEGEE 454
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESMK 729
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
220-422 5.24e-05

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: 46.06  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 220 SELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymikvelEAKMESLKDEInfmrVLYEAELSQMQTHVSDT 299
Cdd:NF033930  157 EELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAE-------EAEIEKLQNEE----VALEAKIAELENQVDNL 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 300 SVVLSmDNNRNLDLDGIIAEVRAQYE-EIARKsKAEVeSWYQIKVQQLQMSADQHGDSLKSTKNE--ISELNRMIQRIRS 376
Cdd:NF033930  226 EKELA-EIDESDSEDYIKEGLRAPLEsELDAK-QAKL-AKKQTELEKLLDSLDPEGKTQDELDKEaaEEELSKKIDELDN 302
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1940128062 377 EIENIKKQTLQASVAD---AEQRGELALKDAYTKRADLEtalqKAKEDL 422
Cdd:NF033930  303 EVAKLEKEVSDLENSDnnvADYYKEALEKDLATKKAELE----KTQKDL 347
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
146-456 1.36e-147

Intermediate filament protein;


Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 425.49  E-value: 1.36e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 146 EREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtSPRNLDPFFETYINALRKNLDTLSNDKGRLQSELKLM 225
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGA-EPSRLYSLYEREIRDLRRQLDQLTVERARLQLEIDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 226 QDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSM 305
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 306 DNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQ- 384
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQk 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1940128062 385 -TLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 456
Cdd:pfam00038 241 aSLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-142 4.15e-34

Keratin type II head;


Pssm-ID: 406589  Cd Length: 160  Bit Score: 126.31  E-value: 4.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  14 GFSSGSAVAGGVKRVAFSSASMSG----------GAGRCSSGGFGSRSLYNLGGHKSISMSVAGSCQGGGYGGAGGFGVG 83
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSCSRsggggggggyGAGGGHGGGFGSRSLYNLGGSKSISISVAGGGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  84 GYGAGFGAGGFGGGFGGSFNGRGG---------------------PGFPVCPAGGIQEVTINQSLLTPLQVEIDPEIQKI 142
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFGGGGfgggggfggggfggggfggggFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
146-453 3.34e-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: 56.60  E-value: 3.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  146 EREQ-IKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSPRNLDpfFETYINALRKNLDTLSNDKGRLQSELKL 224
Cdd:TIGR02168  674 ERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  225 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDvdaaymiKVELEAKMESLKDEINfmrvLYEAELSQMQTHVSDTSVVLS 304
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  305 MDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKVQ--QLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENik 382
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEE-- 898
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062  383 kqtLQASVADAE-QRGEL--ALKDAYTKRADLETALQKAKEDLA----RLMRDYQELMNVKLALDVEIATYRKLLEGE 453
Cdd:TIGR02168  899 ---LSEELRELEsKRSELrrELEELREKLAQLELRLEGLEVRIDnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRR 973
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-451 7.97e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 55.11  E-value: 7.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  201 INALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINF 280
Cdd:COG1196    234 LKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  281 mrvlYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEveswyqikvQQLQMSADQHGDSLKST 360
Cdd:COG1196    314 ----LENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEEL---------EEKLSALLEELEELFEA 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  361 -KNEISELNRMIQRIRSEIENIKKQT--LQASVADAEQRGELA---LKDAYTKRADLETALQKAKEDLARLMRDYQELMN 434
Cdd:COG1196    381 lREELAELEAELAEIRNELEELKREIesLEERLERLSERLEDLkeeLKELEAELEELQTELEELNEELEELEEQLEELRD 460
                          250
                   ....*....|....*..
gi 1940128062  435 VKLALDVEIATYRKLLE 451
Cdd:COG1196    461 RLKELERELAELQEELQ 477
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
195-457 1.43e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 54.34  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  195 PFFETYINALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESL 274
Cdd:COG1196    663 LAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  275 KDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEveSWYQIKVQQLQMSADQHG 354
Cdd:COG1196    743 EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEEL--EEAERRLDALERELESLE 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  355 DSLKSTKNEISELNRMIQRIRSEIENIKKQ--TLQASVADAEQRGELALKdaytKRADLETALQKAKEDLARLMRDYQEL 432
Cdd:COG1196    821 QRRERLEQEIEELEEEIEELEEKLDELEEEleELEKELEELKEELEELEA----EKEELEDELKELEEEKEELEEELREL 896
                          250       260
                   ....*....|....*....|....*
gi 1940128062  433 MNVKLALDVEIATYRKLLEGEECRM 457
Cdd:COG1196    897 ESELAELKEEIEKLRERLEELEAKL 921
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
147-451 2.92e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 53.56  E-value: 2.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  147 REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTtsprnldpfFETYINALRKNLDTLSNDKGRLQSELKLMQ 226
Cdd:COG1196    673 EEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEE---------LERQLEELKRELAALEEELEQLQSRLEELE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  227 DSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFmrvlYEAELSQMQTHVSDTSVVLSMD 306
Cdd:COG1196    744 EELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEE----LEEELEEAERRLDALERELESL 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  307 NNRNLDLDGIIAEVRAQYEEIARK---SKAEVESwYQIKVQQLQMSADQHGDSLKST--------------KNEISELNR 369
Cdd:COG1196    820 EQRRERLEQEIEELEEEIEELEEKldeLEEELEE-LEKELEELKEELEELEAEKEELedelkeleeekeelEEELRELES 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  370 MIQRIRSEIENIKKQTLQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKL 449
Cdd:COG1196    899 ELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEER 978

                   ..
gi 1940128062  450 LE 451
Cdd:COG1196    979 YE 980
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-425 1.57e-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: 51.21  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  144 TAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLqqqttttspRNLDPFFETYINALRKNLDTLSNDKGRLQSELK 223
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEEL---------RLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  224 LMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQthvsdtsvvl 303
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE---------- 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  304 smdnnrnldldgiiaEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQH--GDSLKSTKNEISELNRMIQR-----IRS 376
Cdd:TIGR02168  376 ---------------ELEEQLETLRSKVAQLELQIASLNNEIERLEARLErlEDRRERLQQEIEELLKKLEEaelkeLQA 440
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1940128062  377 EIENIKKQ--TLQASVADAEQRGELALKdaytKRADLETALQKAKEDLARL 425
Cdd:TIGR02168  441 ELEELEEEleELQEELERLEEALEELRE----ELEEAEQALDAAERELAQL 487
PRK01156 PRK01156
chromosome segregation protein; Provisional
134-454 2.16e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 50.67  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 134 EIDPEIQKIRTAE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTT---------TTSPRNLDPFFETYINA 203
Cdd:PRK01156  401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgEEKSNHIINHYNEKKSR 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 204 LRKNLDTLSNDKGRLQSE---LKLMQDSVEDFKT-KYEEEINKRTAAENDfvvLKKDVDAAYMIKvELEAKMESLKDEIN 279
Cdd:PRK01156  481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEInKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYK 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 280 FMRVlyeAELSQMQTHVSDTSVVLSmdnnrNLDLDGIiaevRAQYEEIARKSKAEVESWYQIKVQQLQMSA--------- 350
Cdd:PRK01156  557 SLKL---EDLDSKRTSWLNALAVIS-----LIDIETN----RSRSNEIKKQLNDLESRLQEIEIGFPDDKSyidksirei 624
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 351 DQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQTLQA-SVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDY 429
Cdd:PRK01156  625 ENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
                         330       340
                  ....*....|....*....|....*
gi 1940128062 430 QELMNVKLALDVEIATYRKLLEGEE 454
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESMK 729
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
139-460 2.50e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 50.48  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  139 IQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLEtkwNLLQQ----------------------------------- 183
Cdd:COG1196    574 LDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVR---FVLGDtlvvddleqarrlarklrikyrivtldgdlvepsg 650
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  184 -QTTTTSPRNLDPFFETYINALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYM 262
Cdd:COG1196    651 sITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEE 730
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  263 IKVELEAKMESLKDEINF---MRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEI----------AR 329
Cdd:COG1196    731 ELEQLQSRLEELEEELEEleeELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELeeeleeaerrLD 810
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  330 KSKAEVESWyQIKVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQ--TLQASVADAEQRgelaLKDAYTK 407
Cdd:COG1196    811 ALERELESL-EQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEEleELEAEKEELEDE----LKELEEE 885
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1940128062  408 RADLETAL-------QKAKEDLARLMRDYQELMNVKLALDVEI-ATYRKLLEGEECRMSGE 460
Cdd:COG1196    886 KEELEEELreleselAELKEEIEKLRERLEELEAKLERLEVELpELEEELEEEYEDTLETE 946
46 PHA02562
endonuclease subunit; Provisional
162-412 7.24e-06

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 48.47  E-value: 7.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 162 DKVRFLEQQNKVLETKWNLLQQQTTTtsprnldpfFETYINALRKnldtLSNDKgrlQSELKLMQDSVEDFKTKYEEEIN 241
Cdd:PHA02562  174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRK----KNGEN---IARKQNKYDELVEEAKTIKAEIE 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 242 KRTAAENDFVVLKKDVDAAY----MIKVELEAKMESLKDEINFMRvlyeaELSQMQTHVSDTSvvlsmdnnrnlDLDGII 317
Cdd:PHA02562  238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE-----KGGVCPTCTQQIS-----------EGPDRI 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 318 AEVRAQYEEIARKSKAEveswyQIKVQQLQMSADQHGD---SLKSTKNEISELNRMIQRIRSEIENIKKQTLQASVADAE 394
Cdd:PHA02562  302 TKIKDKLKELQHSLEKL-----DTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
                         250       260
                  ....*....|....*....|...
gi 1940128062 395 QRGELA-----LKDAYTKRADLE 412
Cdd:PHA02562  377 NAEELAklqdeLDKIVKTKSELV 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
119-438 3.65e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  119 QEVTINQSLLTPLQVEIDPEIQKIRTAEREqIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQttttsprnldpffe 198
Cdd:TIGR02168  726 RQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-------------- 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  199 tyINALRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKdvdaaymIKVELEAKMESLKDEI 278
Cdd:TIGR02168  791 --IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEI 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  279 NFMRVLYEAELSQMQTHVsdtsvvlsmdnNRNLDLDGIIAEVRAQYEEIARKSKaEVESwyqiKVQQLQmsadqhgDSLK 358
Cdd:TIGR02168  862 EELEELIEELESELEALL-----------NERASLEEALALLRSELEELSEELR-ELES----KRSELR-------RELE 918
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  359 STKNEISELNRMIQRIRSEIENIKKQtlqasvadAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQELMNVKLA 438
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQER--------LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-451 3.72e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.63  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  201 INALRKNLDTLSNDKGRLQSELKLMQDSVEDFKtKYEEEINKRTAAENDFVVLKKDvdaaymikvELEAKMESLKDEINF 280
Cdd:COG1196    181 LERTEENLERLEDLLEELEKQLEKLERQAEKAE-RYQELKAELRELELALLLAKLK---------ELRKELEELEEELSR 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  281 MRVLYEAELSQMQthvsdtsvvlsmdnnrnlDLDGIIAEVRAQYEEIARKSKAEVESWYQIKvqqlqmsadqhgdslkst 360
Cdd:COG1196    251 LEEELEELQEELE------------------EAEKEIEELKSELEELREELEELQEELLELK------------------ 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  361 kNEISELNRMIQRIRSEIENIKKQTLQASVADAEQRGEL-ALKDAYTKRADLETALQKAKEDLARLMRDYQE-LMNVKLA 438
Cdd:COG1196    295 -EEIEELEGEISLLRERLEELENELEELEERLEELKEKIeALKEELEERETLLEELEQLLAELEEAKEELEEkLSALLEE 373
                          250
                   ....*....|...
gi 1940128062  439 LDVEIATYRKLLE 451
Cdd:COG1196    374 LEELFEALREELA 386
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
220-422 5.24e-05

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: 46.06  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 220 SELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAymikvelEAKMESLKDEInfmrVLYEAELSQMQTHVSDT 299
Cdd:NF033930  157 EELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAE-------EAEIEKLQNEE----VALEAKIAELENQVDNL 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 300 SVVLSmDNNRNLDLDGIIAEVRAQYE-EIARKsKAEVeSWYQIKVQQLQMSADQHGDSLKSTKNE--ISELNRMIQRIRS 376
Cdd:NF033930  226 EKELA-EIDESDSEDYIKEGLRAPLEsELDAK-QAKL-AKKQTELEKLLDSLDPEGKTQDELDKEaaEEELSKKIDELDN 302
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1940128062 377 EIENIKKQTLQASVAD---AEQRGELALKDAYTKRADLEtalqKAKEDL 422
Cdd:NF033930  303 EVAKLEKEVSDLENSDnnvADYYKEALEKDLATKKAELE----KTQKDL 347
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
332-454 7.79e-05

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 44.28  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 332 KAEVESWYQIKVQQLQMS-----ADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQT--LQASVADAEQR---GELAL 401
Cdd:COG1579     3 NNNLKSLLAIQKLDLEKDrleprIKEIRKALKKAKAELEALNKALEALEIELEDLENQVsqLESEIQEIRERikrAEEKL 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1940128062 402 KDAYTKRA--DLETALQKAKEDLARLMRDYQELMNVKLALDVEIATYRKLLEGEE 454
Cdd:COG1579    83 SAVKDERElrALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLE 137
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
172-426 1.98e-04

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


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 43.90  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 172 KVLETKWNLLQQQTTTTSPRNldpffetYINAlRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFV 251
Cdd:COG4477   171 KKLENIEEELSQFVELTSSGD-------YIEA-REVLEEAEEHMIALRSIMERIPSLLAELQTELPGQLQDLKAGYRDMK 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 252 VlkkdvDAAYMIKVELEAKMESLKDEINFMRVLY--------EAELSQMQTHVSDT-----------SVVLSMDNNRNLD 312
Cdd:COG4477   243 E-----EGYHLEHVNIDSRLERLKEQLVENSELLtqleldeaEEELGLIQEKIESLydllereveakNVVEENLPILPDY 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 313 LDGIIAEVRAQYEEIARKSK----AEVESWYQIKVQQLQMSADQHGDSLKSTKNE----ISELNRMIQRIRSEIENIKKQ 384
Cdd:COG4477   318 LEKAKENNEHLKEEIERVKEsyrlAETELGSVRKFEKELKELESVLDEILENIEAqevaYSELQDNLEEIEKALTDIEDE 397
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1940128062 385 tlQASVADAEQRGElalKDAYTKRADLETaLQKAKEDLARLM 426
Cdd:COG4477   398 --QEKVQEHLTSLR---KDELEARENLER-LKSKLHEIKRYM 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
204-432 3.53e-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: 43.52  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  204 LRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEI-NFMR 282
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIeNVKS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  283 VL--YEAELSQMQTHVSdtSVVLSMDNNRNLDLDGIIAEVRAQYEEIarksKAEVESWYQI------KVQQLQMSADQHG 354
Cdd:TIGR02169  759 ELkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKL----EEEVSRIEARlreieqKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062  355 DSLKSTKNEISELNRMIQRIRSEIENIKKQtlQASVADAEQRGELALKDAYTKRADLETALQKAKEDLARLMRDYQEL 432
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGK--KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
264-451 6.76e-04

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: 42.42  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 264 KVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVE-----SW 338
Cdd:pfam05557   4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkKK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 339 YQIKVQQLQMSADQH----GDSLKSTKNEISELNRMIQR-------IRSEIENIKKQ--TLQASVADAEQRGE------L 399
Cdd:pfam05557  84 YLEALNKKLNEKESQladaREVISCLKNELSELRRQIQRaelelqsTNSELEELQERldLLKAKASEAEQLRQnlekqqS 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 400 ALKDAYTKRADLETALQKAKEDLARLMRDYQELMNV------KLALDVEIATYRKLLE 451
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIpelekeLERLREHNKHLNENIE 221
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
134-381 1.29e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  134 EIDPEIQKIRTAEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQTTTTSpRNLDpFFETYINALRKNLDTLSN 213
Cdd:COG1196    786 EKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELE-EKLD-ELEEELEELEKELEELKE 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  214 DKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYMIKVELEAKMESLKDEINFMRVLYEAELSQMQ 293
Cdd:COG1196    864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTL 943
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  294 THVSDTSV-----VLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQIKvqqlqmsadqhgDSLKSTKNEI-SEL 367
Cdd:COG1196    944 ETELEREIerleeEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLL------------EVIEELDKEKrERF 1011
                          250
                   ....*....|....
gi 1940128062  368 NRMIQRIRSEIENI 381
Cdd:COG1196   1012 KETFDKINENFSEI 1025
PRK09039 PRK09039
peptidoglycan -binding protein;
286-424 1.91e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 286 EAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEiARKSKAEVESWYQIKVQQLQMSADQHGD---SLKSTKN 362
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1940128062 363 EISELNRMIQRIRSEIENIKKQ--TLQASVADAEQRGelalKDAYTKRAD----LETALQKAKEDLAR 424
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQlaALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
131-460 2.34e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.61  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 131 LQVEIDPEIQKIRTAEREQIKTLNNKFASFIDKVRF---LEQQNKV----LETKWNLLQQQTTTTSPRN--LDPFFETYI 201
Cdd:PLN03229  434 LEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKeidLEYTEAViamgLQERLENLREEFSKANSQDqlMHPVLMEKI 513
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 202 NALRKNLDTLSNDKGRLQSeLKLMQDSVEDFkTKYEEEINKRTAAENdfvvLKKDVD---AAYMIKVELEAKMESLKDEI 278
Cdd:PLN03229  514 EKLKDEFNKRLSRAPNYLS-LKYKLDMLNEF-SRAKALSEKKSKAEK----LKAEINkkfKEVMDRPEIKEKMEALKAEV 587
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 279 NfmrvlyEAELSQMQTHVSDT-SVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVEswyQIKVQQLQmsadqhgDSL 357
Cdd:PLN03229  588 A------SSGASSGDELDDDLkEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE---QTPPPNLQ-------EKI 651
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 358 KSTKNEIselNRMIQR-IRSEIENIKKQTLQASVADAEQRGELALKDAytkradLETALQKAKEDLARLMrDYQELMNVK 436
Cdd:PLN03229  652 ESLNEEI---NKKIERvIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIAEAL-NSSELKEKF 721
                         330       340
                  ....*....|....*....|....
gi 1940128062 437 LALDVEIATYRKLLEGEECRMSGE 460
Cdd:PLN03229  722 EELEAELAAARETAAESNGSLKND 745
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
122-383 3.98e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 40.03  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  122 TINQSLLTPLQVEIDPEIQKIRTAEREQIK----TLNNKfasfidkvrfleqQNKVLETKWNLLQQQTTTTSpRNLDPFF 197
Cdd:TIGR01612  692 TEDKAKLDDLKSKIDKEYDKIQNMETATVElhlsNIENK-------------KNELLDIIVEIKKHIHGEIN-KDLNKIL 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  198 ETYINAlRKNLDTLSNDKGRLQSELKLMQDSVEDFKTKYEEEINKRTAAENDfvvLKKDVDAAYMIKVELEAKMESLKDE 277
Cdd:TIGR01612  758 EDFKNK-EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062  278 INFMRVLYEAELSQMQTHVsdtsvvlSMDNNRNLDLDgiiaEVRAQYEEIARKSKAEVESwyqikvQQLQMSADQHGDSl 357
Cdd:TIGR01612  834 INEMKFMKDDFLNKVDKFI-------NFENNCKEKID----SEHEQFAELTNKIKAEISD------DKLNDYEKKFNDS- 895
                          250       260
                   ....*....|....*....|....*.
gi 1940128062  358 kstKNEISELNRMIQRIRSEIENIKK 383
Cdd:TIGR01612  896 ---KSLINEINKSIEEEYQNINTLKK 918
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
266-451 5.75e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 39.36  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 266 ELEAKMESLKDEINFMRVLYEAELSQMQTHVsdtsvvLSMDNNRNLDLDGIIAEVRAQYEEIARKSK--AEVESWYQIKV 343
Cdd:COG0419   182 EAKAKIEELEGQLSELLEDIEDLLEALEEEL------KELKKLEEIQEEQEEEELEQEIEALEERLAelEEEKERLEELK 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1940128062 344 QQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIkkQTLQASVADAEQRgELALKDAYTKRADLETALQKAKEDLA 423
Cdd:COG0419   256 ARLLEIESLELEALKIREEELRELERLLEELEEKIERL--EELEREIEELEEE-LEGLRALLEELEELLEKLKSLEERLE 332
                         170       180
                  ....*....|....*....|....*...
gi 1940128062 424 RLMRDYQELMNVKLALDVEIATYRKLLE 451
Cdd:COG0419   333 KLEEKLEKLESELEELAEEKNELAKLLE 360
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH