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Conserved domains on  [gi|109115294|ref|XP_001102045|]
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keratin, type I cytoskeletal 39 [Macaca mulatta]

Protein Classification

intermediate filament family protein( domain architecture ID 11981676)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882
PubMed:  2183847|12596228|28101862

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
95-402 6.64e-115

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 341.13  E-value: 6.64e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   95 NEKETMQILNERLANYLEKVRMLERENAELESKIQEENNKELPVLCPDYLSYYTTIEELQQKILCTKAENSRLVSQIDNT 174
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  175 KLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQLG-ERLHIEV 253
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  254 TAAPSVDLNQVLQEMRCQYESIMETNRKDVEQWFNTQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVELQAQHRMR 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109115294  334 DSQECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLES 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
95-402 6.64e-115

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 341.13  E-value: 6.64e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   95 NEKETMQILNERLANYLEKVRMLERENAELESKIQEENNKELPVLCPDYLSYYTTIEELQQKILCTKAENSRLVSQIDNT 174
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  175 KLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQLG-ERLHIEV 253
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  254 TAAPSVDLNQVLQEMRCQYESIMETNRKDVEQWFNTQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVELQAQHRMR 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109115294  334 DSQECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLES 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-403 4.47e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 4.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   103 LNERLANYLEKVRMLERENAELESKIQ------EENNKELPVLcpdylsyYTTIEELQQKILCTKAENSRLVSQIDNTKL 176
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQeleeklEELRLEVSEL-------EEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   177 TADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELlclknnhkEEINSLQCQLGERLHievtaa 256
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELEAELEELESRLE------ 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   257 psvDLNQVLQEMRcqyesimeTNRKDVEQwfntQIEELNqqvvtssqqqqccqKEIIELRRTVNTLEVELQAQHRMRDSQ 336
Cdd:TIGR02168  376 ---ELEEQLETLR--------SKVAQLEL----QIASLN--------------NEIERLEARLERLEDRRERLQQEIEEL 426

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109115294   337 ECILTETEARYTAL-LTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLESL 403
Cdd:TIGR02168  427 LKKLEEAELKELQAeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 150-408 5.64e-07

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: 51.69  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 150 IEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELlc 229
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 230 lknnhKEEINSLQcQLGERLHIEVTAAPSvDLNQVLQEMRcQYESIMETNRKdveqwfntQIEELNqqvvtssqqqqccq 309
Cdd:COG4942  107 -----AELLRALY-RLGRQPPLALLLSPE-DFLDAVRRLQ-YLKYLAPARRE--------QAEELR-------------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 310 KEIIELRRTVNTLEVELQAQHRMRDSQEciltETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRL 389
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELE----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                        250
                 ....*....|....*....
gi 109115294 390 ECEITTYRSLLESLDGKRP 408
Cdd:COG4942  233 EAEAAAAAERTPAAGFAAL 251
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-403 1.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  94 SNEKETMQILNERLANYLEKVRMLERENAELESKIQ--EENNKELPvlcpdylsyyTTIEELQQKI-----LCTKAENSR 166
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRelEERIEELK----------KEIEELEEKVkelkeLKEKAEEYI 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 167 LVSqidntKLTADDLRAKYEAEVSLRQLvEADANGLKQILNVLTLGKA---DLEAQVQSLKEELLCLKNNHK--EEINSL 241
Cdd:PRK03918 297 KLS-----EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAK 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 242 QCQLgERLHIEVTAAPSVDLNQVLQEMRCQYESIMEtnrkdveqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRTVNT 321
Cdd:PRK03918 371 KEEL-ERLKKRLTGLTPEKLEKELEELEKAKEEIEE------------EISKITARIGELKKEIKELKKAIEELKKAKGK 437

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 322 LEV---ELQAQHRmrdsqecilTETEARYTALLTQIQSLIDNLEAQLAEIRcaleRQNQEYEILLDVKSRLeceiTTYRS 398
Cdd:PRK03918 438 CPVcgrELTEEHR---------KELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESEL----IKLKE 500


                 ....*
gi 109115294 399 LLESL 403
Cdd:PRK03918 501 LAEQL 505
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
95-402 6.64e-115

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 341.13  E-value: 6.64e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   95 NEKETMQILNERLANYLEKVRMLERENAELESKIQEENNKELPVLCPDYLSYYTTIEELQQKILCTKAENSRLVSQIDNT 174
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  175 KLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQLG-ERLHIEV 253
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  254 TAAPSVDLNQVLQEMRCQYESIMETNRKDVEQWFNTQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVELQAQHRMR 333
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109115294  334 DSQECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLES 402
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-403 4.47e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 4.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   103 LNERLANYLEKVRMLERENAELESKIQ------EENNKELPVLcpdylsyYTTIEELQQKILCTKAENSRLVSQIDNTKL 176
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQeleeklEELRLEVSEL-------EEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   177 TADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELlclknnhkEEINSLQCQLGERLHievtaa 256
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELEAELEELESRLE------ 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   257 psvDLNQVLQEMRcqyesimeTNRKDVEQwfntQIEELNqqvvtssqqqqccqKEIIELRRTVNTLEVELQAQHRMRDSQ 336
Cdd:TIGR02168  376 ---ELEEQLETLR--------SKVAQLEL----QIASLN--------------NEIERLEARLERLEDRRERLQQEIEEL 426

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109115294   337 ECILTETEARYTAL-LTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLESL 403
Cdd:TIGR02168  427 LKKLEEAELKELQAeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 150-408 5.64e-07

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: 51.69  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 150 IEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELlc 229
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 230 lknnhKEEINSLQcQLGERLHIEVTAAPSvDLNQVLQEMRcQYESIMETNRKdveqwfntQIEELNqqvvtssqqqqccq 309
Cdd:COG4942  107 -----AELLRALY-RLGRQPPLALLLSPE-DFLDAVRRLQ-YLKYLAPARRE--------QAEELR-------------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 310 KEIIELRRTVNTLEVELQAQHRMRDSQEciltETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRL 389
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELE----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                        250
                 ....*....|....*....
gi 109115294 390 ECEITTYRSLLESLDGKRP 408
Cdd:COG4942  233 EAEAAAAAERTPAAGFAAL 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-401 8.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 8.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294    96 EKETMQILNER--LANYLEKVRMLERENAELESKIQEennkelpvlcpdylsYYTTIEELQQKILCTKAENSRLVSQIDN 173
Cdd:TIGR02168  666 AKTNSSILERRreIEELEEKIEELEEKIAELEKALAE---------------LRKELEELEEELEQLRKELEELSRQISA 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   174 TKLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLK---NNHKEEINSLQCQLGErLH 250
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEELKALREALDE-LR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   251 IEVTaapsvDLNQVLQEMRCQYESiMETNRKDVEQwfntQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVELQAQH 330
Cdd:TIGR02168  810 AELT-----LLNEEAANLRERLES-LERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   331 RMRDSQECILTETEARYTALLTQIQSL----------IDNLEAQLAEIRCAL-----------ERQNQEYEILLDVKSRL 389
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELeskrselrreLEELREKLAQLELRLeglevridnlqERLSEEYSLTLEEAEAL 959

                          330
                   ....*....|..
gi 109115294   390 ECEITTYRSLLE 401
Cdd:TIGR02168  960 ENKIEDDEEEAR 971
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 142-404 1.65e-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: 50.84  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   142 DYLSYYTTIEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKY-EAEVSLRQLvEADANGLKQILNVLTLGKADLEAQV 220
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELsDASRKIGEI-EKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   221 QSLKEELLCLKNNHKE---EINSLQCQLGErLHIEVTAAPSVDLNQVLQEMRCQYESIMETNRKDVEQwfntqIEELNQQ 297
Cdd:TIGR02169  747 SSLEQEIENVKSELKEleaRIEELEEDLHK-LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEAR-----LREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   298 VVTSSQQQQCCQKEIIELRRTVNTLE---VELQAQ-----HRMRDSQEcILTETEARYTAL---LTQIQSLIDNLEAQLA 366
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKeqiKSIEKEienlnGKKEELEE-ELEELEAALRDLesrLGDLKKERDELEAQLR 899

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 109115294   367 EIRCALERQNQEYEILLDVKSRLECEITTYRSLLESLD 404
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-406 1.98e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   151 EELQQKILCTKAENSRLVSQIDNTKLTADDLRAKY-EAEVSLRQLvEADANGLKQILNVLTLGKADLEAQVQSLKEELlc 229
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALaELRKELEEL-EEELEQLRKELEELSRQISALRKDLARLEAEV-- 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   230 lkNNHKEEINSLQCQLGE-RLHIEVTAAPSVDLNQVLQEMrcqyesimETNRKDVEQwfntQIEELNQQVVTSSQQQQCC 308
Cdd:TIGR02168  743 --EQLEERIAQLSKELTElEAEIEELEERLEEAEEELAEA--------EAEIEELEA----QIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   309 QKEIIELRRTVNTLEVELQAQHRMRDSQECILTETEARytalLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSR 388
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          250
                   ....*....|....*...
gi 109115294   389 LECEITTYRSLLESLDGK 406
Cdd:TIGR02168  885 LEEALALLRSELEELSEE 902
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 96-390 6.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  96 EKETMQILNERLANYLEKVRMLERENAELESKIQEENNKelpvlcpdylsyyttIEELQQKILCTKAENSRLVSQIDNTK 175
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELE---------------LEEAQAEEYELLAELARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 176 LTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELlclkNNHKEEINSLQCQLGERLHIEVTA 255
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL----AEAEEALLEAEAELAEAEEELEEL 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 256 ApsvdlNQVLQEMRcqyesimetnrkdveqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVELQAQHRMRDS 335
Cdd:COG1196  385 A-----EELLEALR--------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109115294 336 QECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLE 390
Cdd:COG1196  440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 93-406 5.41e-05

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: 45.78  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   93 NSNEKETMQILNERLANYLEKVRMLERENAELESKIQEENN------KELPVLCPDYLSYYTTIEELQQKILCTKAENSR 166
Cdd:TIGR04523 302 NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  167 LVSQIDNTKLTADDLRAKYeaevslrQLVEADANGLKQILNVLTLGKADLEAQVQSLKEEllclKNNHKEEINSLQCQLG 246
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKI-------QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET----IIKNNSEIKDLTNQDS 450

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  247 E-RLHIEVTAAPSVDLNQVLQEMRCQYESImETNRKDVEQWF---NTQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTL 322
Cdd:TIGR04523 451 VkELIIKNLDNTRESLETQLKVLSRSINKI-KQNLEQKQKELkskEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  323 EVE-LQAQHRMRDSQECILT-ETEARYTALLTQIQSLIDNLEaQLAEIRCALERQNQEYEILLDVKSR----LECEITTY 396
Cdd:TIGR04523 530 ESEkKEKESKISDLEDELNKdDFELKKENLEKEIDEKNKEIE-ELKQTQKSLKKKQEEKQELIDQKEKekkdLIKEIEEK 608

                         330
                  ....*....|
gi 109115294  397 RSLLESLDGK 406
Cdd:TIGR04523 609 EKKISSLEKE 618
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-407 2.47e-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: 43.90  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   103 LNERLANYLEKVRMLERENAELESKIQEeNNKELPvlcpdylSYYTTIEELQQKILCTKAENSRlvSQIDNtkltaddLR 182
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVKSELKE-LEARIE-------ELEEDLHKLEEALNDLEARLSH--SRIPE-------IQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   183 AKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKE---EINSLQCQLGErlhievtaapsv 259
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekEIENLNGKKEE------------ 865

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   260 dlnqvlqemrcqyesimetnrkdveqwFNTQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVELQAQHRMRDSQECI 339
Cdd:TIGR02169  866 ---------------------------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   340 LTETEARYTALLTQIQSLIDN--------------------LEAQLAEIRcALERQN----QEYEI-------LLDVKSR 388
Cdd:TIGR02169  919 LSELKAKLEALEEELSEIEDPkgedeeipeeelsledvqaeLQRVEEEIR-ALEPVNmlaiQEYEEvlkrldeLKEKRAK 997

                          330
                   ....*....|....*....
gi 109115294   389 LECEITTYRSLLESLDGKR 407
Cdd:TIGR02169  998 LEEERKAILERIEEYEKKK 1016
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 96-405 2.99e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 43.41  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  96 EKETMQILNERLANYLEKVRMLE----RENAELESKIQEENNKELPvlcpdylsyytTIEELQQKILCTKAENSRLVSQI 171
Cdd:COG5185  244 ELEDLAQTSDKLEKLVEQNTDLRleklGENAESSKRLNENANNLIK-----------QFENTKEKIAEYTKSIDIKKATE 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 172 DNTKLTAddlraKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNH-----KEEINSLQCQLg 246
Cdd:COG5185  313 SLEEQLA-----AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVelsksSEELDSFKDTI- 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 247 ERLHIEVTAAPsVDLNQVLQEMRCQYESIMETNRKDVEQwFNTQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTLEVEL 326
Cdd:COG5185  387 ESTKESLDEIP-QNQRGYAQEILATLEDTLKAADRQIEE-LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR 464

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109115294 327 QAQHRMRDSQEciLTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLESLDG 405
Cdd:COG5185  465 LEEAYDEINRS--VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 148-378 3.28e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 148 TTIEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKY-EAEVSLRQLVEADANGLKQIlnvltlgkADLEAQVQSLKEE 226
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnELQAELEALQAEIDKLQAEI--------AEAEAEIEERREE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 227 LlclknnhKEEINSLQCQLGERLHIEVTAApSVDLNQVLQemRCQY-ESIMETNRKDVEQwFNTQIEELNQQVVtssqqq 305
Cdd:COG3883   88 L-------GERARALYRSGGSVSYLDVLLG-SESFSDFLD--RLSAlSKIADADADLLEE-LKADKAELEAKKA------ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109115294 306 qccqkeiiELRRTVNTLEVELQAQHRMRDSqeciLTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQE 378
Cdd:COG3883  151 --------ELEAKLAELEALKAELEAAKAE----LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 90-281 3.92e-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: 43.24  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294    90 EGINSNEKETMQILNERLANYLEKVRMLERENAELESKIQE------ENNKELPVLCPDYLSYYTTIEELQQKILCTKAE 163
Cdd:pfam01576  383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSEserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   164 NSRLVSQIDNTK-LTADDLRAKYEAEVSLRQLvEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQ 242
Cdd:pfam01576  463 VSSLESQLQDTQeLLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLE 541

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 109115294   243 cQLGE---RLHIEVTAapsvdLNQVLQEMRCQYESIMETNRK 281
Cdd:pfam01576  542 -ALEEgkkRLQRELEA-----LTQQLEEKAAAYDKLEKTKNR 577
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 92-369 4.39e-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: 43.13  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294    92 INSNEKETMQI---LNERLANYLEKVRMLERENAELESKIQEENN---KELPVLCPDYLSYYTTIEELQQKILCTKAENS 165
Cdd:TIGR02169  246 LASLEEELEKLteeISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEIASLERSIAEKERELEDAEERLA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   166 RLVSQIDNTKLTADDLRAKYEAEVSLRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLK---NNHKEEINSLQ 242
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELK 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   243 CQLgERLHIEvtaapSVDLNQVLQEMRCQYESIMEtnrkdveqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRTVNTL 322
Cdd:TIGR02169  406 REL-DRLQEE-----LQRLSEELADLNAAIAGIEA------------KINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 109115294   323 EVELQAqhrmrdsqeciLTETEARYTALLTQIQSLIDNLEAQLAEIR 369
Cdd:TIGR02169  468 EQELYD-----------LKEEYDRVEKELSKLQRELAEAEAQARASE 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 92-407 6.74e-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: 42.36  E-value: 6.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294    92 INSNEKETMQILNERLAnylekvrmLERENAELESKIQEeNNKELPVLCPDYLSYYTTIEEL--------QQKILCTKAE 163
Cdd:TIGR02169  232 KEALERQKEAIERQLAS--------LEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   164 NSRLVSQIDNTKLTADDL---RAKYEAEvslRQLVEADANGLKQILNVLTLGKADLEAQVQSLKEELlclknnhkeeiNS 240
Cdd:TIGR02169  303 IASLERSIAEKERELEDAeerLAKLEAE---IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-----------ED 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   241 LQCQLGErlhIEVTAAPSVDLNQVLQEmrcqyesimetnrkdveqwfntQIEELNqqvvtssqqqqccqKEIIELRRTVN 320
Cdd:TIGR02169  369 LRAELEE---VDKEFAETRDELKDYRE----------------------KLEKLK--------------REINELKRELD 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   321 TLEVELQaqhrmRDSQEciLTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLL 400
Cdd:TIGR02169  410 RLQEELQ-----RLSEE--LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482


                   ....*..
gi 109115294   401 ESLDGKR 407
Cdd:TIGR02169  483 KELSKLQ 489
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
105-393 1.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  105 ERLANYLEKVRMLERENAELESKIQEENNKELpvLCPDYLSYYTTIEEL---QQKILCTKAENSRLVSQIDNTKLTADDL 181
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELD--ALQERREALQRLAEYswdEIDVASAEREIAELEAELERLDASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  182 RAkyeaevsLRQLVEAdangLKQILNVLTLGKADLEAQVQSLKEELlclkNNHKEEINSLQCQLGerlhiEVTAAPSVDL 261
Cdd:COG4913   688 AA-------LEEQLEE----LEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLE-----AAEDLARLEL 747

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  262 NQVLQEMRcqYESIMETNRKDVEQWFNTQIEELNQqvvtssqqqqccqkeiiELRRTVNTLEvELQAQHRMR---DSQEc 338
Cdd:COG4913   748 RALLEERF--AAALGDAVERELRENLEERIDALRA-----------------RLNRAEEELE-RAMRAFNREwpaETAD- 806

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 109115294  339 ILTETEAR--YTALLTQIQSliDNLEAQLAEIRCALERQNQEYeiLLDVKSRLECEI 393
Cdd:COG4913   807 LDADLESLpeYLALLDRLEE--DGLPEYEERFKELLNENSIEF--VADLLSKLRRAI 859
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
97-407 1.20e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  97 KETMQILNERLANYLEKVRmlerenaELESKIQeennkelpvlcpDYLSyyttieelQQKILCTKAENSRLVSQIdntkl 176
Cdd:COG3206  174 RKALEFLEEQLPELRKELE-------EAEAALE------------EFRQ--------KNGLVDLSEEAKLLLQQL----- 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 177 taDDLRAkyeaevslrQLVEADANglkqilnvltlgKADLEAQVQSLKeellclknnhkeeinslqcqlgERLHIEVTAA 256
Cdd:COG3206  222 --SELES---------QLAEARAE------------LAEAEARLAALR----------------------AQLGSGPDAL 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 257 PSVDLNQVLQEMRCQYESImetnrkdveqwfNTQIEELnqqvvtsSQQQQCCQKEIIELRRTVNTLEVELQAQHRMrdsq 336
Cdd:COG3206  257 PELLQSPVIQQLRAQLAEL------------EAELAEL-------SARYTPNHPDVIALRAQIAALRAQLQQEAQR---- 313

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109115294 337 ecILTETEARYTALLTQIQSLIDNLEAQLAEIRcALERQNQEYeilldvkSRLECEITTYRSLLESLDGKR 407
Cdd:COG3206  314 --ILASLEAELEALQAREASLQAQLAQLEARLA-ELPELEAEL-------RRLEREVEVARELYESLLQRL 374
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-403 1.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  94 SNEKETMQILNERLANYLEKVRMLERENAELESKIQ--EENNKELPvlcpdylsyyTTIEELQQKI-----LCTKAENSR 166
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRelEERIEELK----------KEIEELEEKVkelkeLKEKAEEYI 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 167 LVSqidntKLTADDLRAKYEAEVSLRQLvEADANGLKQILNVLTLGKA---DLEAQVQSLKEELLCLKNNHK--EEINSL 241
Cdd:PRK03918 297 KLS-----EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHElyEEAKAK 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 242 QCQLgERLHIEVTAAPSVDLNQVLQEMRCQYESIMEtnrkdveqwfntQIEELNQQVVTSSQQQQCCQKEIIELRRTVNT 321
Cdd:PRK03918 371 KEEL-ERLKKRLTGLTPEKLEKELEELEKAKEEIEE------------EISKITARIGELKKEIKELKKAIEELKKAKGK 437

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 322 LEV---ELQAQHRmrdsqecilTETEARYTALLTQIQSLIDNLEAQLAEIRcaleRQNQEYEILLDVKSRLeceiTTYRS 398
Cdd:PRK03918 438 CPVcgrELTEEHR---------KELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESEL----IKLKE 500


                 ....*
gi 109115294 399 LLESL 403
Cdd:PRK03918 501 LAEQL 505
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 90-385 3.05e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294    90 EGINSNEKETMQILNERLANYLEKVRMLERENAELESKIQEENNkeLPVLCPDYLSYYTTIEELQQKILCTKAENSRLVS 169
Cdd:TIGR00618  479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN--PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   170 QIDNTKLTADDLRAKYEAEVSLRQLVEADANGLKQILN-VLTLGKADLEAQVQSL------------------------- 223
Cdd:TIGR00618  557 QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVrLQDLTEKLSEAEDMLAceqhallrklqpeqdlqdvrlhlqq 636

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   224 KEELLCLKNNHKEE----------------INSLQCQLGERLHIEVTAAPSV---------DLNQVLQEMRCQYESImET 278
Cdd:TIGR00618  637 CSQELALKLTALHAlqltltqervrehalsIRVLPKELLASRQLALQKMQSEkeqltywkeMLAQCQTLLRELETHI-EE 715

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   279 NRKDVEQWFN---TQIEELNqqvvTSSQQQQCCQKEIIELRRTVNTLEVELQAQhrmRDSQECILTETEARYTALLTQIQ 355
Cdd:TIGR00618  716 YDREFNEIENassSLGSDLA----AREDALNQSLKELMHQARTVLKARTEAHFN---NNEEVTAALQTGAELSHLAAEIQ 788

                          330       340       350
                   ....*....|....*....|....*....|...
gi 109115294   356 SLIDNLEA---QLAEIRCALERQNQEYEILLDV 385
Cdd:TIGR00618  789 FFNRLREEdthLLKTLEAEIGQEIPSDEDILNL 821
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-392 3.75e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294    95 NEKETM-QILNERLANylekvrmLERENAELEskiqeennkelpvlcpdylsyyTTIEELQQKILCTKAENSRLVSQIDN 173
Cdd:TIGR02168  298 SRLEQQkQILRERLAN-------LERQLEELE----------------------AQLEELESKLDELAEELAELEEKLEE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   174 TKLTADDLRAKYEAEVSLRQlveadanglkqilnVLTLGKADLEAQVQSLKEELlclkNNHKEEINSLQCQLgERLHIEV 253
Cdd:TIGR02168  349 LKEELESLEAELEELEAELE--------------ELESRLEELEEQLETLRSKV----AQLELQIASLNNEI-ERLEARL 409

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   254 TAApSVDLNQVLQEMRCQYESIMETNRKDVEQWFNTQIEELNqqvvtssqqqqccqkEIIELRRTVNTLEVELQAQHRMR 333
Cdd:TIGR02168  410 ERL-EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE---------------ELQEELERLEEALEELREELEEA 473

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 109115294   334 DSQECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECE 392
Cdd:TIGR02168  474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
46 PHA02562
endonuclease subunit; Provisional
 114-403 3.80e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 114 VRMLERENAELESKIQEeNNKELPVLcpDYLsyyttIEELQQKIlctKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQ 193
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRE-LNQQIQTL--DMK-----IDHIQQQI---KTYNKNIEEQRKKNGENIARKQNKYDELVEEAK 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 194 LVEADANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKeeinslQCQLGERLHIEVTAAPSVdlNQVLQEMRCQYE 273
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE------QFQKVIKMYEKGGVCPTC--TQQISEGPDRIT 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294 274 SImETNRKDVEQWF---NTQIEELNQQVVtssqqqqccqkEIIELRRTVNTLEVELQAQHrmrdsQECILTETEARytal 350
Cdd:PHA02562 303 KI-KDKLKELQHSLeklDTAIDELEEIMD-----------EFNEQSKKLLELKNKISTNK-----QSLITLVDKAK---- 361

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109115294 351 ltQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEItTYRSLLESL 403
Cdd:PHA02562 362 --KVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK-YHRGIVTDL 411
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 98-403 9.98e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.50  E-value: 9.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294   98 ETMQILNERLANYLEKVRMLERENAELESKIQEENNKELPVlcPDYLSyyttIEELQQKILCTKA---ENSRLVSQ-IDN 173
Cdd:PRK10929   58 EERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSV--PPNMS----TDALEQEILQVSSqllEKSRQAQQeQDR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  174 TKLTADDL----RAKYEAEvslRQLVEADANgLKQILNVLT-LGKAD---LEAQVQSLKE-----ELLCLKNNHKEEINs 240
Cdd:PRK10929  132 AREISDSLsqlpQQQTEAR---RQLNEIERR-LQTLGTPNTpLAQAQltaLQAESAALKAlvdelELAQLSANNRQELA- 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  241 lqcqlgeRLHIEVTAAPSVDLNQVLQEMRCQYESI-----------------------------METNRkDVEQWFNTQI 291
Cdd:PRK10929  207 -------RLRSELAKKRSQQLDAYLQALRNQLNSQrqreaeralestellaeqsgdlpksivaqFKINR-ELSQALNQQA 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109115294  292 EELNQQVVTSSQQQqccqKEIIELRRTVNTLEVelQAQHrmrdsqeciLTETEARYTALLTQIQSLID-----NLEAQLA 366
Cdd:PRK10929  279 QRMDLIASQQRQAA----SQTLQVRQALNTLRE--QSQW---------LGVSNALGEALRAQVARLPEmpkpqQLDTEMA 343

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109115294  367 EIRCA-------LERQNQEYEILLDVKSRLECE--------ITTYRSLLESL 403
Cdd:PRK10929  344 QLRVQrlryedlLNKQPQLRQIRQADGQPLTAEqnrildaqLRTQRELLNSL 395
 
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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