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Conserved domains on  [gi|229463044|sp|P02533|]
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RecName: Full=Keratin, type I cytoskeletal 14; AltName: Full=Cytokeratin-14; Short=CK-14; AltName: Full=Keratin-14; Short=K14

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;
114-425 6.28e-149

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 427.03  E-value: 6.28e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  114 SEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNA 193
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  194 RLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVG-GDVNVEM 272
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  273 DAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMK 352
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229463044  353 ASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 425
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
114-425 6.28e-149

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 427.03  E-value: 6.28e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  114 SEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNA 193
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  194 RLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVG-GDVNVEM 272
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  273 DAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMK 352
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229463044  353 ASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 425
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
214-420 1.61e-09

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: 60.46  E-value: 1.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   214 VEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEK 293
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   294 MAEKNRKDAEEWFFTKTE------ELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYC 367
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEaeaeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 229463044   368 M---QLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 420
Cdd:TIGR02168  842 DleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
195-413 1.57e-06

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: 50.15  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 195 LAADDFRTKYETELNlrmSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKK---NHEEEMNALRGQVGgDVNVE 271
Cdd:COG4942   16 AAQADAAAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 272 MDAapgvdLSRILNEMRDQYEKM---AEKNRKDAEEWFFTKTEELN---REVATNSELVQSGKSEISELRRTMQNLEIEL 345
Cdd:COG4942   92 IAE-----LRAELEAQKEELAELlraLYRLGRQPPLALLLSPEDFLdavRRLQYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229463044 346 QSQLSMKASLENSLEETKGrycmQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIA 413
Cdd:COG4942  167 AELEAERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
114-425 6.28e-149

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 427.03  E-value: 6.28e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  114 SEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNA 193
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  194 RLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVG-GDVNVEM 272
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  273 DAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMK 352
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229463044  353 ASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 425
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
214-420 1.61e-09

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: 60.46  E-value: 1.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   214 VEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEK 293
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   294 MAEKNRKDAEEWFFTKTE------ELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYC 367
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEaeaeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 229463044   368 M---QLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 420
Cdd:TIGR02168  842 DleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
206-420 4.45e-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: 4.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   206 TELNLRMS-VEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHE-----------------EEMNALRGQVgGD 267
Cdd:TIGR02168  270 EELRLEVSeLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaqleeleskldelaEELAELEEKL-EE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   268 VNVEMDAapgvdLSRILNEMRDQYEKMAEKNRKDAEEWfftktEELNREVATNSELVQSGKSEISELRRTMQNLEIELQS 347
Cdd:TIGR02168  349 LKEELES-----LEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229463044   348 QLSMKASLENSLEETkgrycmQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 420
Cdd:TIGR02168  419 LQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
169-414 8.97e-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: 8.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   169 IEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAY 248
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   249 L---KKNHEEEMNALRGQVGGDVNvEMDAapgvdLSRILNEMRDQYE-------------KMAEKNRKDAEEWFftktEE 312
Cdd:TIGR02168  773 AeeeLAEAEAEIEELEAQIEQLKE-ELKA-----LREALDELRAELTllneeaanlrerlESLERRIAATERRL----ED 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   313 LNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMigsvEEQLAQLRCEME 392
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELE 918
                          250       260
                   ....*....|....*....|..
gi 229463044   393 QQNQEYKILLDVKTRLEQEIAT 414
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDN 940
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
195-413 1.57e-06

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: 50.15  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 195 LAADDFRTKYETELNlrmSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKK---NHEEEMNALRGQVGgDVNVE 271
Cdd:COG4942   16 AAQADAAAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 272 MDAapgvdLSRILNEMRDQYEKM---AEKNRKDAEEWFFTKTEELN---REVATNSELVQSGKSEISELRRTMQNLEIEL 345
Cdd:COG4942   92 IAE-----LRAELEAQKEELAELlraLYRLGRQPPLALLLSPEDFLdavRRLQYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 229463044 346 QSQLSMKASLENSLEETKGrycmQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIA 413
Cdd:COG4942  167 AELEAERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
232-426 3.66e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 49.35  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  232 RADLEMQIESLKEELAYLKKNHEEEMN-ALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAE------- 303
Cdd:pfam05557   4 LIESKARLSQLQNEKKQMELEHKRARIeLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkkk 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044  304 --EWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRY------CMQLAQIQE 375
Cdd:pfam05557  84 ylEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAseaeqlRQNLEKQQS 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 229463044  376 MIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQ--EIATYRRLLEGEDAHL 426
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHL 216
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
221-420 1.14e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 221 LRRVLDELTLARADLEMQIESLKEELAylkkNHEEEMNALRGQVGGdVNVEMDAApgvDLSRILNEMRDQYEKmAEKNRK 300
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 301 DAEEWFFTKTEELNREVATNSELVQSgkSEISELRRTMQNLEIELQSQLS-----------MKASLENSLEETKGRYCMQ 369
Cdd:COG3206  237 EAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEAQRI 314
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 229463044 370 LAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVK---TRLEQEIATYRRLLE 420
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
114-414 6.52e-05

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: 45.49  E-value: 6.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   114 SEKVTMQN----LNDRLASYLDKVRALEEANADL-EVKIRDWYQRQRPAEIKDYSPYFKTIEDLRN--KILTATVDNANV 186
Cdd:pfam15921  486 AKKMTLESsertVSDLTASLQEKERAIEATNAEItKLRSRVDLKLQELQHLKNEGDHLRNVQTECEalKLQMAEKDKVIE 565
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   187 LL--QIDN-ARLAADDFRTKYETELNlRMSVEADINGLRRVLDELTLAR-------ADLEMQIESLKEELAYLKKNHEEE 256
Cdd:pfam15921  566 ILrqQIENmTQLVGQHGRTAGAMQVE-KAQLEKEINDRRLELQEFKILKdkkdakiRELEARVSDLELEKVKLVNAGSER 644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   257 MNALRgqvggDVNVEMDAAPG-VDLSRI-LNEMRDQYEKMAEKNRKDAEEwfftkteelnREVATNSELVQ--SGKSEIS 332
Cdd:pfam15921  645 LRAVK-----DIKQERDQLLNeVKTSRNeLNSLSEDYEVLKRNFRNKSEE----------METTTNKLKMQlkSAQSELE 709
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   333 ELRRTMQNLEIELQSQLSMKASLENSLEETKGrycmQLAQIQEMIGSVEEQlaqlrceMEQQNQEYKILLDVKTRLEQEI 412
Cdd:pfam15921  710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKIQFLEEA-------MTNANKEKHFLKEEKNKLSQEL 778

                   ..
gi 229463044   413 AT 414
Cdd:pfam15921  779 ST 780
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
119-424 4.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 119 MQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRqrpaeikdyspyfktIEDLRNKILTATvdnanvlLQIDNARLAAD 198
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAE---------------LEELRLELEELE-------LELEEAQAEEY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 199 DFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRgqvggdvnvemdaapgv 278
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE----------------- 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 279 DLSRILNEMRDQYEKMAEKNRKDAEEWfftktEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENS 358
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229463044 359 LEETKgrycMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDA 424
Cdd:COG1196  430 LAELE----EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
119-366 4.59e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   119 MQNLNDRLASYLDKVRALEEANADLEVKIRdwYQRQRpaeikdyspyfktIEDLRNKILTATVDNANVLLQIDNARLAAD 198
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQ--ILRER-------------LANLERQLEELEAQLEELESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   199 DFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLkknhEEEMNALRGQVGgdVNVEMDAAPGV 278
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIE--RLEARLERLED 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044   279 DLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKS---EISELRRTMQNLEIELQSQLSMKASL 355
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEElreELEEAEQALDAAERELAQLQARLDSL 494
                          250
                   ....*....|.
gi 229463044   356 ENSLEETKGRY 366
Cdd:TIGR02168  495 ERLQENLEGFS 505
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
221-398 6.62e-03

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: 38.79  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 221 LRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNvEMDAApgvdlSRILNEMRDQYEKMAEKNRK 300
Cdd:COG5185  386 IESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATS-SNEEV-----SKLLNELISELNKVMREADE 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 301 DAEEWFFTKTEELNREVATN----SELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEET-----KGRYCMQLA 371
Cdd:COG5185  460 ESQSRLEEAYDEINRSVRSKkedlNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESlkdfmRARGYAHIL 539
                        170       180
                 ....*....|....*....|....*..
gi 229463044 372 QIQEMIGSVEEQLAQLRCEMEQQNQEY 398
Cdd:COG5185  540 ALENLIPASELIQASNAKTDGQAANLR 566
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
213-386 7.71e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 7.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 213 SVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKN---HEEEMNALRGQVGGDVNVE-MDAAPGVDLSRILN--- 285
Cdd:COG3883   34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGses 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229463044 286 --EMRDQYEKMAEKNRKDAEEwfFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETK 363
Cdd:COG3883  114 fsDFLDRLSALSKIADADADL--LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
                        170       180
                 ....*....|....*....|...
gi 229463044 364 GRYCMQLAQIQEMIGSVEEQLAQ 386
Cdd:COG3883  192 AAAEAQLAELEAELAAAEAAAAA 214
 
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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