NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767993777|ref|XP_011522716|]
View 

keratin, type I cytoskeletal 25 isoform X1 [Homo sapiens]

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
76-389 3.71e-117

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 345.37  E-value: 3.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   76 NEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRgldhDYSRYFPIIDDLKNQIIASTTSNANAVLQ 155
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  156 IDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQC-AAGGNV 234
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  235 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSL 314
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767993777  315 LATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDD 389
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
76-389 3.71e-117

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 345.37  E-value: 3.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   76 NEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRgldhDYSRYFPIIDDLKNQIIASTTSNANAVLQ 155
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  156 IDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQC-AAGGNV 234
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  235 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSL 314
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767993777  315 LATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDD 389
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-376 2.40e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   135 IDDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLS---EE 211
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerlEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   212 MTYLKKNHKEEMQVLQcaagGNVNVEMNAApgVDLTVLLNNMRAEYEAL----------AEQNRRDAEAWfnEKSAS-LQ 280
Cdd:TIGR02168  773 AEEELAEAEAEIEELE----AQIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT--ERRLEdLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   281 QQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESnycaQLAQIQAQIGALEEQLHQVRTETEGQ 360
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS----ELEELSEELRELESKRSELRRELEEL 920

                          250
                   ....*....|....*.
gi 767993777   361 KleyEQLLDIKLHLEK 376
Cdd:TIGR02168  921 R---EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 254-380 7.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 254 RAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESN-- 331
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767993777 332 -YCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIET 380
Cdd:COG1196  306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 171-368 4.92e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 38.20  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 171 ENELALHQSVEADVNGLRRVLDeitlcrtDLEIQYETLSEEMTYLKKNHKEEMQVLqcaaggNVNVEMNAAPGVDLTVLL 250
Cdd:cd00176   36 EALLKKHEALEAELAAHEERVE-------ALNELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 251 NNMRAEYEALAEQnrRDAEAWFNEKSASLQQQ-ISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLEcsltetE 329
Cdd:cd00176  103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767993777 330 SNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLL 368
Cdd:cd00176  175 EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
76-389 3.71e-117

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 345.37  E-value: 3.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   76 NEKVTMQNLNDRLASYLDSVHALEEANADLEQKIKGWYEKFGPGSCRgldhDYSRYFPIIDDLKNQIIASTTSNANAVLQ 155
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  156 IDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQC-AAGGNV 234
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  235 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSL 314
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767993777  315 LATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIETYCLLIGGDD 389
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 169-389 2.03e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  169 KYENELALHQSVEADVNGlrrVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLQCAAGGNVNVEMNAAPGV---- 244
Cdd:pfam05483 173 KYEYEREETRQVYMDLNN---NIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqi 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  245 --------DLTVLLNNMRAEYEALAEQNRRDAE--AWFNEK-----------------SASLQQQISEDVGATTSARNEL 297
Cdd:pfam05483 250 tekenkmkDLTFLLEESRDKANQLEEKTKLQDEnlKELIEKkdhltkeledikmslqrSMSTQKALEEDLQIATKTICQL 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  298 TEMKRTlqtlEIELQSLLATKHSLecSLTETESNYCA---QLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHL 374
Cdd:pfam05483 330 TEEKEA----QMEELNKAKAAHSF--VVTEFEATTCSleeLLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403

                         250
                  ....*....|....*
gi 767993777  375 EKEIETYCLLIGGDD 389
Cdd:pfam05483 404 EVELEELKKILAEDE 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 135-376 2.40e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   135 IDDLKNQIIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLS---EE 211
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEerlEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   212 MTYLKKNHKEEMQVLQcaagGNVNVEMNAApgVDLTVLLNNMRAEYEAL----------AEQNRRDAEAWfnEKSAS-LQ 280
Cdd:TIGR02168  773 AEEELAEAEAEIEELE----AQIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT--ERRLEdLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   281 QQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESnycaQLAQIQAQIGALEEQLHQVRTETEGQ 360
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS----ELEELSEELRELESKRSELRRELEEL 920

                          250
                   ....*....|....*.
gi 767993777   361 KleyEQLLDIKLHLEK 376
Cdd:TIGR02168  921 R---EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 254-380 7.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 254 RAEYEALAEQNRRDAEAWFNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESN-- 331
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767993777 332 -YCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIET 380
Cdd:COG1196  306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 296-377 8.86e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 8.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 296 ELTEMKRTLQTLEIELQSLLAtkhslecsltETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLE 375
Cdd:COG0542  412 ELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481


                 ..
gi 767993777 376 KE 377
Cdd:COG0542  482 QR 483
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 155-361 1.00e-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: 41.29  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 155 QIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKEEMQVLqcAAGGNV 234
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--AELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 235 NVEMNAAPGvdLTVLLNN-------MRAEY-EALAEQNRRDAEAwFNEKSASLQQQISEdvgaTTSARNELTEMKRTLQT 306
Cdd:COG4942  113 LYRLGRQPP--LALLLSPedfldavRRLQYlKYLAPARREQAEE-LRADLAELAALRAE----LEAERAELEALLAELEE 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767993777 307 LEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQK 361
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-368 1.12e-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: 40.90  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 273 NEKSASLQQQISEdvgattsARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETE---SNYCAQLAQIQAQIGALEEQ 349
Cdd:COG4942   19 ADAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALArriRALEQELAALEAELAELEKE 91

                         90
                 ....*....|....*....
gi 767993777 350 LHQVRTETEGQKLEYEQLL 368
Cdd:COG4942   92 IAELRAELEAQKEELAELL 110
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
249-367 1.24e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.99  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 249 LLNNM--RAEYEAL--AEQNRRDAEAWFNEKSASLQQ-QISE---DVGATTSARNELT-EMKRTLQTLEIELQSLLATkh 319
Cdd:COG3524  166 LVNQLseRAREDAVrfAEEEVERAEERLRDAREALLAfRNRNgilDPEATAEALLQLIaTLEGQLAELEAELAALRSY-- 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767993777 320 slecsltETESNycAQLAQIQAQIGALEEQLHQVRTE----TEGQKL-----EYEQL 367
Cdd:COG3524  244 -------LSPNS--PQVRQLRRRIAALEKQIAAERARltgaSGGDSLasllaEYERL 291
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
239-368 3.12e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 239 NAAPGVDLTVLLNNMRAEYEALaEQNRRDAEAWFNEKS---ASLQQQISEdvgattsARNEL-TEMKRTLQTLEIELQSL 314
Cdd:COG3206  254 DALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHpdvIALRAQIAA-------LRAQLqQEAQRILASLEAELEAL 325

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767993777 315 LATKHSLECSLTETESNYcAQLAQIQAQIGALEEQLhQVRTETegqkleYEQLL 368
Cdd:COG3206  326 QAREASLQAQLAQLEARL-AELPELEAELRRLEREV-EVAREL------YESLL 371
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
245-379 3.58e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777  245 DLTVLLNNMRAEYEALAEQnRRDAEawfnEKSASLQQQISEDVGAT-TSARNELTEMKRTLQTLEIELQSLLATKHSLEC 323
Cdd:COG4913   299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGL 373

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767993777  324 SLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKLHLEKEIE 379
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 171-368 4.92e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 38.20  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 171 ENELALHQSVEADVNGLRRVLDeitlcrtDLEIQYETLSEEMTYLKKNHKEEMQVLqcaaggNVNVEMNAAPGVDLTVLL 250
Cdd:cd00176   36 EALLKKHEALEAELAAHEERVE-------ALNELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 251 NNMRAEYEALAEQnrRDAEAWFNEKSASLQQQ-ISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLEcsltetE 329
Cdd:cd00176  103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767993777 330 SNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLL 368
Cdd:cd00176  175 EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 187-379 7.47e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   187 LRRVLDEITlcrtDLEIQYETLSEEMTYLKKNHKEEMQVLQcaaggnvnvemnaapgvDLTVLLNNMRAEYEALAEQnrr 266
Cdd:TIGR02169  676 LQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELS-----------------DASRKIGEIEKEIEQLEQE--- 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   267 daEAWFNEKSASLQQQISEdvgattsARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYC-AQLAQIQAQIGA 345
Cdd:TIGR02169  732 --EEKLKERLEELEEDLSS-------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShSRIPEIQAELSK 802

                          170       180       190
                   ....*....|....*....|....*....|....
gi 767993777   346 LEEQlhqvRTETEGQKLEYEQLLDiKLHLEKEIE 379
Cdd:TIGR02169  803 LEEE----VSRIEARLREIEQKLN-RLTLEKEYL 831
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 142-361 8.32e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 8.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 142 IIASTTSNANAVLQIDNARLTADDFRLKYENELALHQSVEADVNGLRRVLDEITLCRTDLEIQYETLSEEMTYLKKNHKE 221
Cdd:COG3883    4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 222 EMQVLQCAAggnVNVEMNAAPGVDLTVLLNN-------MRAEY-EALAEQNRRDAEAwfnekSASLQQQISEDVGATTSA 293
Cdd:COG3883   84 RREELGERA---RALYRSGGSVSYLDVLLGSesfsdflDRLSAlSKIADADADLLEE-----LKADKAELEAKKAELEAK 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767993777 294 RNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQK 361
Cdd:COG3883  156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
254-384 8.51e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777 254 RAEYEALAEQNRRDAEAwfNEKSASLQQQISEDVGATTSARNELTEmkrtlQTLEIELQSLLATKHSLEcsltetesnyc 333
Cdd:COG4717  384 EEELRAALEQAEEYQEL--KEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELE----------- 445

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767993777 334 AQLAQIQAQIGALEEQLHQVRTETEGQKL--EYEQLLDIKLHLEKEIETYCLL 384
Cdd:COG4717  446 EELEELREELAELEAELEQLEEDGELAELlqELEELKAELRELAEEWAALKLA 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-361 8.66e-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: 38.50  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   199 TDLEIQYETLSEEMTYLKKNHKEEMQVLQCAAGGNVNVE---MNAAPGVDLTV----LLNNMRAEYEALAEQNRRDAEAW 271
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVAQLElqiaSLNNEIERLEARLERLEDRRERL 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993777   272 FNEKSASLQQQISEDVGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLH 351
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499

                          170
                   ....*....|
gi 767993777   352 QVRTETEGQK 361
Cdd:TIGR02168  500 NLEGFSEGVK 509
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH