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Conserved domains on  [gi|269849769|sp|P13645|]
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RecName: Full=Keratin, type I cytoskeletal 10; AltName: Full=Cytokeratin-10; Short=CK-10; AltName: Full=Keratin-10; Short=K10

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

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;
145-454 7.60e-123

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 364.63  E-value: 7.60e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  145 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 224
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  225 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 303
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  304 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQL 383
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269849769  384 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
145-454 7.60e-123

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 364.63  E-value: 7.60e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  145 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 224
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  225 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 303
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  304 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQL 383
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269849769  384 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-448 2.70e-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: 2.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   201 KTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEEL 280
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   281 AYLKKNHEEEMKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWfNEKSKELTTEIDNNIEQISS 360
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   361 YKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYcvqlSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKI 440
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                   ....*...
gi 269849769   441 RLENEIQT 448
Cdd:TIGR02168  933 GLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
236-454 3.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 236 LKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPgvdLT 315
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 316 QLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAE 395
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269849769 396 TEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
46 PHA02562
endonuclease subunit; Provisional
206-449 1.63e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 206 LKNQILNLTTDNANILLQIDNARLAADDFRlKYENEvaLRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKK 285
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYN-KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 286 NHEEEMKDLRNVSTGDVNVEMNaapgVDLTQLLNNMRSQY-------EQLAEQNRKDAEAwfNEKSKELTT---EIDNNI 355
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSK----IEQFQKVIKMYEKGgvcptctQQISEGPDRITKI--KDKLKELQHsleKLDTAI 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 356 EQISSYKSEITELRRNVQaleiELQSQLA-LKQSLEASLAetegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 434
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
                        250
                 ....*....|....*
gi 269849769 435 LLDIKIRLENEIQTY 449
Cdd:PHA02562 391 IVKTKSELVKEKYHR 405
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
145-454 7.60e-123

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 364.63  E-value: 7.60e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  145 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 224
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  225 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 303
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  304 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQL 383
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269849769  384 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-448 2.70e-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: 2.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   201 KTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEEL 280
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   281 AYLKKNHEEEMKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWfNEKSKELTTEIDNNIEQISS 360
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   361 YKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYcvqlSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKI 440
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                   ....*...
gi 269849769   441 RLENEIQT 448
Cdd:TIGR02168  933 GLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
236-454 3.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 236 LKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPgvdLT 315
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 316 QLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAE 395
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269849769 396 TEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
256-454 5.68e-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: 49.67  E-value: 5.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   256 RRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNV----------------------EMNAAPGVD 313
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrkdlarleaeveqleERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   314 LTQLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASL 393
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269849769   394 AETEGRYCV---QLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:TIGR02168  834 AATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
242-454 1.58e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 242 VALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRnvstgdvnvemnaapgvDLTQLLNNM 321
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-----------------EAQAEEYEL 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 322 RSQYEQLAEQNRKDAEawfneKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYC 401
Cdd:COG1196  294 LAELARLEQDIARLEE-----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269849769 402 VQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-454 7.43e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 201 KTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYE----NEVALRQSVEADINGLRRV----------LDELTLTK 266
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAELARLEQDIARLeerrreleerLEELEEEL 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 267 ADLEMQIESLTEELAYLKKNHEEEMKDLRnvstgdvnvemnaapgvDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKE 346
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELE-----------------EAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 347 LT---------TEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRycvqLSQIQAQISALEEQ 417
Cdd:COG1196  389 LEalraaaelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE----EAELEEEEEALLEL 464
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 269849769 418 LQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG1196  465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
208-451 3.42e-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: 43.21  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 208 NQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNH 287
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 288 EEEMKDLRNV-----STGDVNVEMNAAPGVDLTQLLNNMRSqYEQLAEQNRkdaeawfnekskeltteidnniEQISSYK 362
Cdd:COG4942  100 EAQKEELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARR----------------------EQAEELR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 363 SEITELRRNVQALEIELQSQLALKQSLEASLAETEgrycVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRL 442
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                 ....*....
gi 269849769 443 ENEIQTYRS 451
Cdd:COG4942  233 EAEAAAAAE 241
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
255-454 3.85e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 255 LRRVLDELTLTKADLEMQIESLTEELAylkkNHEEEMKDLRNvSTGDVNVEMNAApgvDLTQLLNNMRSQYEQlAEQNRK 334
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQ-KNGLVDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 335 DAEAWFNEKSKELTTEID-----NNIEQISSYKSEITELRRNVQALE----------IELQSQLAlkqSLEASLAETEGR 399
Cdd:COG3206  237 EAEARLAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIA---ALRAQLQQEAQR 313
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 269849769 400 YCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:COG3206  314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
357-452 4.46e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 357 QISSYKSEITELRRNVQALEIELQsqlALKQSLEASLAEtegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQLL 436
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKE---ALKKEQDEASFE-------RLAELRDELAELEEELEALKARWEAEKELIEEIQ 474
                         90
                 ....*....|....*.
gi 269849769 437 DIKIRLENEIQTYRSL 452
Cdd:COG0542  475 ELKEELEQRYGKIPEL 490
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
313-448 5.00e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   313 DLTQLLNNMRSQYEQLAEQNRKdaeawFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEAS 392
Cdd:TIGR02169  713 DASRKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 269849769   393 LAETegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQT 448
Cdd:TIGR02169  788 LSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
195-452 5.35e-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: 43.09  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  195 DYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAaddfRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIE 274
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK----LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  275 SLTEELAYLK---KNHEEEMKDLRNVSTGDVN--------VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNE- 342
Cdd:TIGR04523 236 KKQQEINEKTteiSNTQTQLNQLKDEQNKIKKqlsekqkeLEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSe 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769  343 ------KSKELTTEIDNNIEQISSYKSEITELRRNVQALE---IELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISA 413
Cdd:TIGR04523 316 lknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 269849769  414 LEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSL 452
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
246-424 8.95e-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: 41.06  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 246 QSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAApgvdltqllnnmRSQY 325
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK------------KYEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 326 EQLAEQNRKDAEAwfnekskeLTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYCVQLS 405
Cdd:COG1579   81 QLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
                        170
                 ....*....|....*....
gi 269849769 406 QIQAQISALEEQLQQIRAE 424
Cdd:COG1579  153 ELEAELEELEAEREELAAK 171
46 PHA02562
endonuclease subunit; Provisional
206-449 1.63e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 206 LKNQILNLTTDNANILLQIDNARLAADDFRlKYENEvaLRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKK 285
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYN-KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 286 NHEEEMKDLRNVSTGDVNVEMNaapgVDLTQLLNNMRSQY-------EQLAEQNRKDAEAwfNEKSKELTT---EIDNNI 355
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSK----IEQFQKVIKMYEKGgvcptctQQISEGPDRITKI--KDKLKELQHsleKLDTAI 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 356 EQISSYKSEITELRRNVQaleiELQSQLA-LKQSLEASLAetegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 434
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
                        250
                 ....*....|....*
gi 269849769 435 LLDIKIRLENEIQTY 449
Cdd:PHA02562 391 IVKTKSELVKEKYHR 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
250-454 2.14e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   250 ADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTgdvnvEMNAAPGV--DLTQLLNNMRSQYEQ 327
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE-----EIEELQKElyALANEISRLEQQKQI 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   328 LAEQnrkdaEAWFNEKSKELTTEIDNNieqissyKSEITELRRNVQALEIELQSQLALKQSLEASLAETEgrycvqlsqi 407
Cdd:TIGR02168  307 LRER-----LANLERQLEELEAQLEEL-------ESKLDELAEELAELEEKLEELKEELESLEAELEELE---------- 364
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 269849769   408 qAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 454
Cdd:TIGR02168  365 -AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
223-426 2.82e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 223 QIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNV----- 297
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 298 ----STGDVNVEMNAApgvDLTQLLNNMrSQYEQLAEQNRKDAEAwfnekSKELTTEIDNNIEQISSYKSEITELRRNVQ 373
Cdd:COG3883   97 rsggSVSYLDVLLGSE---SFSDFLDRL-SALSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELE 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269849769 374 ALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETE 426
Cdd:COG3883  168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
341-436 3.12e-03

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: 40.13  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769 341 NEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGrycvQLSQIQAQISALEEQLQQ 420
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAE 94
                         90
                 ....*....|....*.
gi 269849769 421 IRAETECQNTEYQQLL 436
Cdd:COG4942   95 LRAELEAQKEELAELL 110
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
146-451 5.99e-03

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: 39.72  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   146 EKVTMQN----LNDRLASYLDKVRALEESNYEL-------EGKIKEWY-----EKHGNSHQGEPR----DYSKYYKTIDD 205
Cdd:pfam15921  487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQhlkneGDHLRNVQTECEalklQMAEKDKVIEI 566
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   206 LKNQILNLTT-----DNANILLQIDNARLAAD--DFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLemqIESLTE 278
Cdd:pfam15921  567 LRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEinDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSE 643
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   279 ELAYLKKNHEEEMKDLRNVSTGDVNvemnaapgvdltqlLNNMRSQYEQLAEQnrkdaeawFNEKSKELTTEIDNNIEQI 358
Cdd:pfam15921  644 RLRAVKDIKQERDQLLNEVKTSRNE--------------LNSLSEDYEVLKRN--------FRNKSEEMETTTNKLKMQL 701
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269849769   359 SSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGrycvQLSQIQAQISALEEQLQQIRAE----TECQNTEYQQ 434
Cdd:pfam15921  702 KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQE 777
                          330       340
                   ....*....|....*....|
gi 269849769   435 LLDI---KIRLENEIQTYRS 451
Cdd:pfam15921  778 LSTVateKNKMAGELEVLRS 797
 
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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