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Conserved domains on  [gi|119395754|ref|NP_000415|]
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keratin, type II cytoskeletal 5 [Homo sapiens]

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;
167-480 1.04e-158

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 456.30  E-value: 1.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  167 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRN 246
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  247 MQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLS 326
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  327 MDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQ 406
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395754  407 CANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECR 480
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
16-164 4.46e-27

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.05  E-value: 4.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   16 SFSTASAITPSVSRTSFTSVSRSGGGGGGGFgrvslAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGY 95
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGG-----GGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   96 GFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPG------------FPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQR 163
Cdd:pfam16208  76 GGGFGGGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFggggfggrggfgGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQR 155


                  .
gi 119395754  164 V 164
Cdd:pfam16208 156 V 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
167-480 1.04e-158

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 456.30  E-value: 1.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  167 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRN 246
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  247 MQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLS 326
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  327 MDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQ 406
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395754  407 CANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECR 480
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
16-164 4.46e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.05  E-value: 4.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   16 SFSTASAITPSVSRTSFTSVSRSGGGGGGGFgrvslAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGY 95
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGG-----GGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   96 GFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPG------------FPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQR 163
Cdd:pfam16208  76 GGGFGGGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFggggfggrggfgGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQR 155


                  .
gi 119395754  164 V 164
Cdd:pfam16208 156 V 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-491 1.60e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   164 VRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSE 243
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   244 LRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKdvdaaymNKVELEAKVDALMDEINFmkmfFDAELSQMQTHVSDTSV 323
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKA----LREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   324 VLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEAEswyqtkyeelqqtagrhgdDLRNTKHEISEMNRMIQRLRAEIDNV 403
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESELEAL 878

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   404 KKQCANLQNAIADAE---------------QRGEL--ALKDARNKLAELEEALQKAKQDMARLLR----EYQELMNTKLA 462
Cdd:TIGR02168  879 LNERASLEEALALLRseleelseelrelesKRSELrrELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEA 958

                          330       340       350
                   ....*....|....*....|....*....|.
gi 119395754   463 LDVEIATYRKLLEGEECRLSGE--GVGPVNI 491
Cdd:TIGR02168  959 LENKIEDDEEEARRRLKRLENKikELGPVNL 989
PRK09039 PRK09039
peptidoglycan -binding protein;
308-456 1.26e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 50.73  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 308 DAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEI-ANRSRteAESWYQTKYEELQQTAGRHGD---DLRNTK 383
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSR--LQALLAELAGAGAAAEGRAGElaqELDSEK 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395754 384 HEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGelalKDARNKLAELEEALQKAkqdmarLLREYQEL 456
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVA------LAQRVQEL 192
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 339-478 3.77e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 339 IAEVKAQYEEIANRSRTEAESW--YQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIAD 416
Cdd:COG1196  262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119395754 417 AEQRGELA---LKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEE 478
Cdd:COG1196  342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 345-481 4.17e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   345 QYEEIANRSRTEA-ESWY-------QTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIAD 416
Cdd:smart00787 118 QFQLVKTFARLEAkKMWYewrmkllEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE 197

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119395754   417 AEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQEL-------MNTKLALDVEIATYRKLLegEECRL 481
Cdd:smart00787 198 LEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELeskiedlTNKKSELNTEIAEAEKKL--EQCRG 267
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
167-480 1.04e-158

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 456.30  E-value: 1.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  167 EEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRqNLEPLFEQYINNLRRQLDSIVGERGRLDSELRN 246
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPS-RLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  247 MQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLS 326
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  327 MDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQ 406
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395754  407 CANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECR 480
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
16-164 4.46e-27

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 107.05  E-value: 4.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   16 SFSTASAITPSVSRTSFTSVSRSGGGGGGGFgrvslAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGY 95
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSSSRRGGGGGG-----GGGGGGGGFGSRSLYNLGGSKSISISVAGGGSRPGSGFGFGGGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   96 GFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPG------------FPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQR 163
Cdd:pfam16208  76 GGGFGGGFGGGGGGGFGGGGGFGGGFGGGGYGGGGFggggfggrggfgGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQR 155


                  .
gi 119395754  164 V 164
Cdd:pfam16208 156 V 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-491 1.60e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   164 VRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEplFEQYINNLRRQLDSIVGERGRLDSE 243
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   244 LRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKdvdaaymNKVELEAKVDALMDEINFmkmfFDAELSQMQTHVSDTSV 323
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKA----LREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   324 VLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEAEswyqtkyeelqqtagrhgdDLRNTKHEISEMNRMIQRLRAEIDNV 403
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESELEAL 878

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   404 KKQCANLQNAIADAE---------------QRGEL--ALKDARNKLAELEEALQKAKQDMARLLR----EYQELMNTKLA 462
Cdd:TIGR02168  879 LNERASLEEALALLRseleelseelrelesKRSELrrELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEA 958

                          330       340       350
                   ....*....|....*....|....*....|.
gi 119395754   463 LDVEIATYRKLLEGEECRLSGE--GVGPVNI 491
Cdd:TIGR02168  959 LENKIEDDEEEARRRLKRLENKikELGPVNL 989
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 156-482 7.52e-08

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: 55.46  E-value: 7.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   156 QIDPSIQRVRtEEREQIKTLNNKFASFIDKVRflEQQNKVLDTKWTLLQEQGTKTVRQNLE-PLFEQYINNLRRQLDSIV 234
Cdd:TIGR02169  167 EFDRKKEKAL-EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQALLKEKREYEgYELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   235 GERGRLDSELRNMQDLVEDFKNKYE------DEINKRTTA--ENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMK-- 304
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEer 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   305 -MFFDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIanRSRTEAESwyqTKYEELQQTAGRHGDDLRNTK 383
Cdd:TIGR02169  324 lAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--RAELEEVD---KEFAETRDELKDYREKLEKLK 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   384 HEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRG---ELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTK 460
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                          330       340
                   ....*....|....*....|..
gi 119395754   461 LALDVEIATYRKLLEGEECRLS 482
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAEAQAR 500
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 220-480 1.19e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 55.12  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   220 EQYINNLRRQLDS---IVGERGRLDSELrnmqdLVEdfKNKYEDEINKRTTAENEFVMLKKDVDAAYMnkvELEAKVDal 296
Cdd:pfam15921  561 DKVIEILRQQIENmtqLVGQHGRTAGAM-----QVE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVS-- 628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   297 mdeinfmkmffDAELSQMQThVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEA--ESWYQTKYEELQQTAGR 374
Cdd:pfam15921  629 -----------DLELEKVKL-VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEvlKRNFRNKSEEMETTTNK 696

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   375 HGDDLRNTKHEISE---------------------MNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELaLKDARNKLA 433
Cdd:pfam15921  697 LKMQLKSAQSELEQtrntlksmegsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLS 775

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 119395754   434 ELEEALQKAKQDMA---RLLREYQELMNTKLAlDVEIATYRKLLEGEECR 480
Cdd:pfam15921  776 QELSTVATEKNKMAgelEVLRSQERRLKEKVA-NMEVALDKASLQFAECQ 824
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 335-472 4.63e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 4.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   335 LDSIIAEVKAQYEEIANRSRTEAESWYQTKYE--ELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQN 412
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395754   413 AIADAEQRGELA---LKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 472
Cdd:TIGR02168  324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
PRK09039 PRK09039
peptidoglycan -binding protein;
308-456 1.26e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 50.73  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 308 DAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEI-ANRSRteAESWYQTKYEELQQTAGRHGD---DLRNTK 383
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSR--LQALLAELAGAGAAAEGRAGElaqELDSEK 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395754 384 HEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGelalKDARNKLAELEEALQKAkqdmarLLREYQEL 456
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRRLNVA------LAQRVQEL 192
PRK01156 PRK01156
chromosome segregation protein; Provisional
 157-478 1.39e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.44  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 157 IDPS-IQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQ------GTKTVRQNLEPLFEQYINNLRR- 228
Cdd:PRK01156 402 IDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKSNHIINHYNEKKSRl 481

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 229 --QLDSIVGERGRLDSELRNMQDLVEDFK----NKYEDEINKRTTAENEfvmLKKDVDAAYMNKvELEAKVDALMDEINF 302
Cdd:PRK01156 482 eeKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARAD---LEDIKIKINELK-DKHDKYEEIKNRYKS 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 303 MKMffdAELSQMQTHVSDTSVVLSmdnnrNLDLDSIIA---EVKAQYEEIANRSRtEAESWYQTKYEELQQTAGRHGDD- 378
Cdd:PRK01156 558 LKL---EDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIENEa 628

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 379 --LRNTKHEISEMNRMIQRLRAEIDNVKKQCANLqNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQEL 456
Cdd:PRK01156 629 nnLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL 707

                        330       340
                 ....*....|....*....|..
gi 119395754 457 MNTKLALDVEIATYRKLLEGEE 478
Cdd:PRK01156 708 RTRINELSDRINDINETLESMK 729
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 226-482 3.82e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   226 LRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEI---NF 302
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvKS 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   303 MKMFFDAELSQMQTHVSdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-ANRSRTEAeswyqtKYEELQQTAGRHGDDLRN 381
Cdd:TIGR02169  759 ELKELEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   382 TKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRgelaLKDARNKLAELEEALQKAKQDMARLLREYQELMNTKL 461
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906

                          250       260
                   ....*....|....*....|.
gi 119395754   462 ALDVEIATYRKLLEGEECRLS 482
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLE 927
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 184-441 3.09e-05

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: 47.35  E-value: 3.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   184 DKVRFLEQQNKVlDTKWTLLQEQGTKTVRQNLEPLFeqyiNNLRRQLDSIVGERGRLDSELRN-MQDLVEDFKNK----- 257
Cdd:TIGR01612  694 DKAKLDDLKSKI-DKEYDKIQNMETATVELHLSNIE----NKKNELLDIIVEIKKHIHGEINKdLNKILEDFKNKekels 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   258 --------------------------YEDEINKRTTAENEfvmLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAEL 311
Cdd:TIGR01612  769 nkindyakekdelnkykskiseiknhYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   312 SQMQTHVsdtsvvlSMDNNRNLDLDSiiaeVKAQYEEIANRSRTEAESWYQTKYEelqqtagrhgDDLRNTKHEISEMNR 391
Cdd:TIGR01612  846 NKVDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAEISDDKLNDYE----------KKFNDSKSLINEINK 904

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 119395754   392 MIQRLRAEIDNVKKQCANLQNAIADAEqrgelALKDARNKLAELEEALQK 441
Cdd:TIGR01612  905 SIEEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 339-478 3.77e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 339 IAEVKAQYEEIANRSRTEAESW--YQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIAD 416
Cdd:COG1196  262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119395754 417 AEQRGELA---LKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEE 478
Cdd:COG1196  342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
46 PHA02562
endonuclease subunit; Provisional
 184-452 4.04e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.55  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 184 DKVRFLEQQNKVLDTKWTLLQEQgTKTvrqnleplFEQYINNLRRQLDSIVgergrldSELRNMQD-LVEDFKNkYEDEI 262
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ-IKT--------YNKNIEEQRKKNGENI-------ARKQNKYDeLVEEAKT-IKAEI 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 263 NKRTTAENEFVMLKKDVDAAyMNKVELE-AKVDALMDEIN-FMKMFFDAEL--SQMQThVSDTsvvlsmdnnrnldlDSI 338
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAA-LNKLNTAaAKIKSKIEQFQkVIKMYEKGGVcpTCTQQ-ISEG--------------PDR 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 339 IAEVKAQYEEIanrsrteaeswyQTKYEELQQtagrHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAE 418
Cdd:PHA02562 301 ITKIKDKLKEL------------QHSLEKLDT----AIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK 364

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 119395754 419 ---QRGELALKDARNKLAELEEALQKAKQDMARLLRE 452
Cdd:PHA02562 365 aaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
220-475 6.10e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 220 EQYIN-NLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDeinkrTTAENEFVMLKKDVDAAYMNKVELEAKVDALMD 298
Cdd:COG3206  159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 299 EINFMKmffdAELSQMQTHVSDTSVVLSMDNNrnldlDSIIAEVKAQYEEIanrsrteaeswyQTKYEELQQTAGrhgdd 378
Cdd:COG3206  234 ELAEAE----ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAEL------------EAELAELSARYT----- 287

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 379 lrntkheisEMNRMIQRLRAEIDNVKKQcanLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARL---LREYQE 455
Cdd:COG3206  288 ---------PNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRR 355

                        250       260
                 ....*....|....*....|..
gi 119395754 456 LMNtklalDVEIA--TYRKLLE 475
Cdd:COG3206  356 LER-----EVEVAreLYESLLQ 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
339-455 6.22e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 339 IAEVKAQYEEIANRsRTEAESWYQTKYEELQQTAGRHgdDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAE 418
Cdd:COG4717  390 ALEQAEEYQELKEE-LEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119395754 419 QRGELA-----LKDARNKLAELEE---ALQKAKQDMARLLREYQE 455
Cdd:COG4717  467 EDGELAellqeLEELKAELRELAEewaALKLALELLEEAREEYRE 511
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
335-472 6.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 335 LDSIIAEVKAQYEEIANRSRTEAEswYQTKYEELQQTAGRHGDDLRN--TKHEISEMNRMIQRLRAEIDNVKKQCANLQN 412
Cdd:COG4717  376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELRE 453

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 413 AIADAEQRGELALKDARnkLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 472
Cdd:COG4717  454 ELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
334-482 9.19e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  334 DLDSIIAEVKAQYEEIANRsRTEAEswyqTKYEELQQT-AGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQC----- 407
Cdd:COG4913   299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLaalgl 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  408 ---------ANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEgEE 478
Cdd:COG4913   374 plpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA-EA 452


                  ....
gi 119395754  479 CRLS 482
Cdd:COG4913   453 LGLD 456
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 196-484 9.28e-05

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 45.62  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 196 LDTKWTLLQEQGTKTVRQN--LEPLFEQYINNLRRQLDSIVGERGRLDSeLRNMQDLVEDF-KNKYEDEINKRTTAenef 272
Cdd:PLN03229 484 LQERLENLREEFSKANSQDqlMHPVLMEKIEKLKDEFNKRLSRAPNYLS-LKYKLDMLNEFsRAKALSEKKSKAEK---- 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 273 vmLKKDVD---AAYMNKVELEAKVDALMDEINFMKMFFDAEL--------SQMQTHVSD--TSVVLSMDnnrnLDLDSII 339
Cdd:PLN03229 559 --LKAEINkkfKEVMDRPEIKEKMEALKAEVASSGASSGDELdddlkekvEKMKKEIELelAGVLKSMG----LEVIGVT 632

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 340 AEVKAQYEEIANRSrteaeswYQTKYEELQQTAGRHGDDLRNTkheiSEMNRMIQRLRAEidnvkkqcanlqnaIADAEQ 419
Cdd:PLN03229 633 KKNKDTAEQTPPPN-------LQEKIESLNEEINKKIERVIRS----SDLKSKIELLKLE--------------VAKASK 687

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119395754 420 RGELALKDARNKL-AELEEALQKAKQDMArlLREYQElmntklALDVEIATYRKLLEGEECRLSGE 484
Cdd:PLN03229 688 TPDVTEKEKIEALeQQIKQKIAEALNSSE--LKEKFE------ELEAELAAARETAAESNGSLKND 745
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 267-472 1.09e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 267 TAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKmffdAELSQMQTHVSDTSVvlSMDNNRNlDLDSIIAEVKAQY 346
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----EEYNELQAELEALQA--EIDKLQA-EIAEAEAEIEERR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 347 EEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNtkheISEMNRMIQRLRAEIDNV---KKQCANLQNAIADAEQRGEL 423
Cdd:COG3883   86 EELGERARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADADLLEELkadKAELEAKKAELEAKLAELEA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119395754 424 ALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 472
Cdd:COG3883  162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 223-442 1.16e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 223 INNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAymnKVELEAKVDALMDEINF 302
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 303 MK----------MFFDAE-LSQMQTHVSDTSVVLSMDNNrnldldsIIAEVKAQYEEIANrsrteAESWYQTKYEELQQT 371
Cdd:COG3883   95 LYrsggsvsyldVLLGSEsFSDFLDRLSALSKIADADAD-------LLEELKADKAELEA-----KKAELEAKLAELEAL 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119395754 372 AGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKA 442
Cdd:COG3883  163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 377-456 1.64e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 377 DDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRgelaLKDARNKLAELEEALQKAKQDMARLLREYQEL 456
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 161-449 1.73e-04

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: 45.04  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   161 IQRVRTEEREQIKTLNNK---FASFIDKVRFLEQQNKVLD----------TKWTLLQEQGTKTVRQNLEPLFEQYINNLR 227
Cdd:TIGR01612  598 INKLKLELKEKIKNISDKneyIKKAIDLKKIIENNNAYIDelakispyqvPEHLKNKDKIYSTIKSELSKIYEDDIDALY 677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   228 RQLDSIVGErgrldSELRNMQD--LVEDFKNKYEDEINKRTTAENEFVMLkkdvdaaymNKVELEAKVDALMDEINFMKM 305
Cdd:TIGR01612  678 NELSSIVKE-----NAIDNTEDkaKLDDLKSKIDKEYDKIQNMETATVEL---------HLSNIENKKNELLDIIVEIKK 743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   306 FFDAELS---------------QMQTHVSDTSvvlsmdnNRNLDLD---SIIAEVKAQYEE---IANRSRTEAESWYQTK 364
Cdd:TIGR01612  744 HIHGEINkdlnkiledfknkekELSNKINDYA-------KEKDELNkykSKISEIKNHYNDqinIDNIKDEDAKQNYDKS 816

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   365 YEELQQTAGRHGD------DLRNTKHEI-SEMNRMI---QRLRAEIDNVKKQCANLQNAIADAEQRGELA-----LKDAR 429
Cdd:TIGR01612  817 KEYIKTISIKEDEifkiinEMKFMKDDFlNKVDKFInfeNNCKEKIDSEHEQFAELTNKIKAEISDDKLNdyekkFNDSK 896

                          330       340
                   ....*....|....*....|
gi 119395754   430 NKLAELEEALQKAKQDMARL 449
Cdd:TIGR01612  897 SLINEINKSIEEEYQNINTL 916
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
335-478 1.90e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 335 LDSIIAEVKAQYEEIANRSRT-----EAESWYQtKYEELQQTAGRHGDDLRNTKHEISEmnrmIQRLRAEIDNVKKQCAN 409
Cdd:COG4717  100 LEEELEELEAELEELREELEKlekllQLLPLYQ-ELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAE 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119395754 410 LQNAIADAEQRGELAlkdARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEE 478
Cdd:COG4717  175 LQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 335-475 2.45e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 335 LDSIIAEVKAQYEEIANRSRTeaeswYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVK--KQCANLQN 412
Cdd:COG1579   22 LEHRLKELPAELAELEDELAA-----LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQK 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119395754 413 AIADAEQRGELA---LKDARNKLAELEEALQKAKQDMARLLREYQELmntKLALDVEIATYRKLLE 475
Cdd:COG1579   97 EIESLKRRISDLedeILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-459 2.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  227 RRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAymnkvELEAKVDALMDEInfmkmf 306
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAEL------ 677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  307 fdaelsqmqthvsdtsvvlsmdnnRNLDLDS-IIAEVKAQYEEiANRSRTEAESwyqtKYEELQQTAGRHgddlrntKHE 385
Cdd:COG4913   678 ------------------------ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKE 721

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119395754  386 ISEMNRMIQRLRAEIDNVKKQCANLQNAIADaEQRGELALKDARNKLAE-LEEALQKAKQDMARLLREYQELMNT 459
Cdd:COG4913   722 LEQAEEELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRA 795
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 204-449 3.14e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   204 QEQGTKTVRQNLE-----PLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKD 278
Cdd:pfam01576  474 QELLQEETRQKLNlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   279 VDAAYMNKVELEAKVDALmdeinfmkmffDAELSQMQTHVSDTSVVLsmDNNRNL---------DLDSIIAEVK---AQY 346
Cdd:pfam01576  554 LEALTQQLEEKAAAYDKL-----------EKTKNRLQQELDDLLVDL--DHQRQLvsnlekkqkKFDQMLAEEKaisARY 620

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   347 EEiaNRSRTEAESwyqTKYEELQQTAGRHGDDLRNTKHEISEMNRMiqrLRAEI-------DNVKKQCANLQNAIADAEQ 419
Cdd:pfam01576  621 AE--ERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQ---LRAEMedlvsskDDVGKNVHELERSKRALEQ 692

                          250       260       270
                   ....*....|....*....|....*....|
gi 119395754   420 rgelALKDARNKLAELEEALQKAKQDMARL 449
Cdd:pfam01576  693 ----QVEEMKTQLEELEDELQATEDAKLRL 718
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 160-475 3.57e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  160 SIQRVRTEEREQIKTLNNKF-------ASFIDKVRFLEQQNKVLDTKWTLLQEQgTKTVRQNLEPLfEQYINNLRRQLDS 232
Cdd:TIGR04523  58 NLDKNLNKDEEKINNSNNKIkileqqiKDLNDKLKKNKDKINKLNSDLSKINSE-IKNDKEQKNKL-EVELNKLEKQKKE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  233 IVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDvdaaymnKVELEAKVDALMDEINFMKMFFDAELS 312
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE-------KLNIQKNIDKIKNKLLKLELLLSNLKK 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  313 QMQTHVSDTSVVLSMDNNRNlDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYE--ELQQTAGRHGDDLRNTKHEISEMN 390
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNN-QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnKIKKQLSEKQKELEQNNKKIKELE 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  391 RMIQRLRAEIDNVKKQ-CANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIAT 469
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367


                  ....*.
gi 119395754  470 YRKLLE 475
Cdd:TIGR04523 368 KQNEIE 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 196-456 5.08e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   196 LDTKWTLLQEQGTKTVRqnleplFEQYINNLRR-QLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVM 274
Cdd:TIGR02168  198 LERQLKSLERQAEKAER------YKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   275 LKKDVDAAYMNKVELEAKVDALMDEIN---FMKMFFDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAN 351
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   352 R--SRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQC----ANLQNAIADAEQRG---- 421
Cdd:TIGR02168  352 EleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerleDRRERLQQEIEELLkkle 431

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 119395754   422 ELALKDARNKLAELEEALQKAKQDMARLLREYQEL 456
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQEELERLEEALEEL 466
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 236-472 5.19e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 5.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 236 ERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKmffdAELSQMQ 315
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 316 THVSDTSVVLSMDNNRnldlDSIIAEVKAQYEEIANRSRTeaesWYQTKYEELQQTAgrhgDDLRNTKHEIsemnrmiQR 395
Cdd:COG4942  104 EELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQ----YLKYLAPARREQA----EELRADLAEL-------AA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119395754 396 LRAEIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRK 472
Cdd:COG4942  165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 150-473 6.28e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  150 LTPLNLQIDPSIQRVRTEERE------QIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgtKTVRQNLEPLFEQYI 223
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVElnklekQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ--KEELENELNLLEKEK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  224 NNLRRQLDSIVGERGRLDSELRNMQDLVEDFKnKYEDEINKrttAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFM 303
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISE---LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  304 KmffdAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIANRsrtEAESWYQTKYEELQQTAgrhgDDLRNTK 383
Cdd:TIGR04523 259 K----DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ---KEQDWNKELKSELKNQE----KKLEEIQ 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  384 HEISEMNRMIQRLRAEIDNVKKQCANLQNaiaDAEQRgelalkdaRNKLAELEEALQKAKQDMARLLREYQELMNTKLAL 463
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSES---ENSEK--------QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396

                         330
                  ....*....|
gi 119395754  464 DVEIATYRKL 473
Cdd:TIGR04523 397 ESKIQNQEKL 406
PRK12704 PRK12704
phosphodiesterase; Provisional
 340-455 6.35e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 340 AEVKAQYEEIANRSRTEAE-----SWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAI 414
Cdd:PRK12704  58 ALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119395754 415 ADAEQRGE----LALKDARNKLaeLEEALQKAKQDMARLLREYQE 455
Cdd:PRK12704 138 EEQLQELErisgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
165-475 9.09e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 165 RTEE-REQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQgtktvRQNLEPLFEQyINNLRRQLDSIVGERGRLDSE 243
Cdd:PRK03918 187 RTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKEE-IEELEKELESLEGSKRKLEEK 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 244 LRNMQDLVEDFKNKYED------EINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDaELSQMQTH 317
Cdd:PRK03918 261 IRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEER 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 318 VSDTSVVLSMDNNRNLDLD------SIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNR 391
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 392 MIQRLRAEIDNVKK---QCAnLQNAIADAEQRGELaLKDARNKLAELEEALQKAKQDMARLLREYQELmNTKLALDVEIA 468
Cdd:PRK03918 420 EIKELKKAIEELKKakgKCP-VCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELI 496


                 ....*..
gi 119395754 469 TYRKLLE 475
Cdd:PRK03918 497 KLKELAE 503
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
223-457 1.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 223 INNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENefvmLKKDVDAAYMNKVELEAKVDALMDEINF 302
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRD 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 303 MKMFFDaELSQMQTHVSDTSVVLSMDNN----RNLDLDSIIAEVKAQYEEI---ANRSRTEAESW------YQTKYEELQ 369
Cdd:PRK02224 284 LRERLE-ELEEERDDLLAEAGLDDADAEaveaRREELEDRDEELRDRLEECrvaAQAHNEEAESLredaddLEERAEELR 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 370 QTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALK---DARNKLAELEEALQKAKQDm 446
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTARER- 441

                        250
                 ....*....|.
gi 119395754 447 arlLREYQELM 457
Cdd:PRK02224 442 ---VEEAEALL 449
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
331-486 1.59e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 331 RNLDLDSIIAEVKAQY------EEIANRSRTEAESwyqtKYEELQQTAGRHGDDLRNtkhEISEMNRMIQRLRAEIDNVK 404
Cdd:COG2433  361 PDVDRDEVKARVIRGLsieealEELIEKELPEEEP----EAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEELE 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 405 KQCANLQNAIADAEQRGELALKDARNKLAELEEaLQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEEcrlSGE 484
Cdd:COG2433  434 AELEEKDERIERLERELSEARSEERREIRKDRE-ISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH---SGE 509


                 ..
gi 119395754 485 GV 486
Cdd:COG2433  510 LV 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 334-478 1.71e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 334 DLDSIIAEVKAQYEEIANRSRtEAESWYQTKYEELQQTAgrhgDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNA 413
Cdd:COG1196  236 ELEAELEELEAELEELEAELE-ELEAELAELEAELEELR----LELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119395754 414 IADAEQRgelaLKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEE 478
Cdd:COG1196  311 RRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 335-475 1.72e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 335 LDSIIAEVKAQYEEIANRSRTEAESW--YQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQN 412
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELeeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395754 413 AIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLE 475
Cdd:COG1196  324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 352-482 2.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 352 RSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQ---RGELALKDA 428
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRREL 314

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119395754 429 RNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLS 482
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
339-482 2.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 339 IAEVKAQYEEIANRSRTEAEswyqtkYEELQQtagrhgddlrntkhEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAE 418
Cdd:COG4717   70 LKELKELEEELKEAEEKEEE------YAELQE--------------ELEELEEELEELEAELEELREELEKLEKLLQLLP 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119395754 419 QRGElaLKDARNKLAELEEALQKAKQDmarlLREYQELMNTKLALDVEIATYRKLLEGEECRLS 482
Cdd:COG4717  130 LYQE--LEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLS 187
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 239-460 2.20e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 239 RLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEInfmkmffdAELSQMQTHV 318
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--------KKYEEQLGNV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 319 SdtsvvlsmdNNRnlDLDSIIAEVkaqyeEIANRSRTEAESwyqtkyeelqqtagrhgddlrntkhEISEMNRMIQRLRA 398
Cdd:COG1579   86 R---------NNK--EYEALQKEI-----ESLKRRISDLED-------------------------EILELMERIEELEE 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395754 399 EIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDM-ARLLREYQELMNTK 460
Cdd:COG1579  125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIpPELLALYERIRKRK 187
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 162-457 2.45e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 40.65  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  162 QRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPlfEQYINNLRRQLDSIVGERGRLD 241
Cdd:pfam07888  72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH--EARIRELEEDIKTLTQRVLERE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  242 SELRNMQDLVEDFKNKYEDE-------INKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFD------ 308
Cdd:pfam07888 150 TELERMKERAKKAGAQRKEEeaerkqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtahrke 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  309 AELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQyeeianRSRTEAE---------------------------SWY 361
Cdd:pfam07888 230 AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ------RDRTQAElhqarlqaaqltlqladaslalregraRWA 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  362 QTKyEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEidNVKkqcanLQNAIADAEQRGELALKDARNKLAELEEALQK 441
Cdd:pfam07888 304 QER-ETLQQSAEADKDRIEKLSAELQRLEERLQEERME--REK-----LEVELGREKDCNRVQLSESRRELQELKASLRV 375

                         330
                  ....*....|....*.
gi 119395754  442 AKQDMARLLREYQELM 457
Cdd:pfam07888 376 AQKEKEQLQAEKQELL 391
PRK11281 PRK11281
mechanosensitive channel MscK;
340-447 3.34e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  340 AEVKAQYEEIANRSRTEAESwyQTKYEELQQTAgRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADA-- 417
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTL-ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtr 115

                          90       100       110
                  ....*....|....*....|....*....|
gi 119395754  418 EQRGELALKDARNKLAELEEALQKAKQDMA 447
Cdd:PRK11281  116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLA 145
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 345-481 4.17e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   345 QYEEIANRSRTEA-ESWY-------QTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIAD 416
Cdd:smart00787 118 QFQLVKTFARLEAkKMWYewrmkllEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDE 197

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119395754   417 AEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQEL-------MNTKLALDVEIATYRKLLegEECRL 481
Cdd:smart00787 198 LEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELeskiedlTNKKSELNTEIAEAEKKL--EQCRG 267
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 161-460 5.02e-03

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  161 IQRVRTEEREQIKTLNNKFASfidkvrfLEQQNKVLDTKWTLLQE-----------QGTKTVRQNLEPLFEQYINNLRRQ 229
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVE-------LEELKKILAEDEKLLDEkkqfekiaeelKGKEQELIFLLQAREKEIHDLEIQ 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  230 LDSIVGERGRLDSELRNMQDLVEDFKNKyedeiNKRTTAENEFVMLKKDVDAAYMNKVELEAKVDalMDEINFMKMFFDA 309
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLK-----NIELTAHCDKLLLENKELTQEASDMTLELKKH--QEDIINCKKQEER 531

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754  310 ELSQMQThVSDTSVVLsmdnnRNlDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLR--NTKHEIS 387
Cdd:pfam05483 532 MLKQIEN-LEEKEMNL-----RD-ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIE 604

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395754  388 EMNRMIQRLRAEIDNVKKQcanlqnaiADAEQRGELALKDARNKLaELEeaLQKAKQDMARLLREYQELMNTK 460
Cdd:pfam05483 605 NKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKL-ELE--LASAKQKFEEIIDNYQKEIEDK 666
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
238-449 7.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 238 GRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDaELSQMQTH 317
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754 318 VSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEI-ANRSRTEAESWYQTKYEELqqtagrhGDDLRNTKHEISEMNRMIQRL 396
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELeEKVKELKELKEKAEEYIKL-------SEFYEEYLDELREIEKRLSRL 319

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119395754 397 RAEIDNVKKQCANLQNAIADAEQRGELaLKDARNKLAELEE---ALQKAKQDMARL 449
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKK-LKELEKRLEELEErheLYEEAKAKKEEL 374
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 352-486 7.59e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395754   352 RSRTEAESWYQTKYEELQQTAgrhgddlrntkHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALKD---- 427
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLR-----------ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieql 728

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119395754   428 ------ARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGV 486
Cdd:TIGR02169  729 eqeeekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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