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Conserved domains on  [gi|1958789929|ref|XP_038935273|]
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keratin, type II cytoskeletal 4 isoform X2 [Rattus norvegicus]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

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

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
1-197 1.20e-81

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 247.91  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   1 MIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQI 80
Cdd:pfam00038 117 LARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  81 KVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGELALKDAYTKRADLETALQKAK 160
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958789929 161 EDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 197
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
1-197 1.20e-81

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 247.91  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   1 MIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQI 80
Cdd:pfam00038 117 LARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  81 KVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGELALKDAYTKRADLETALQKAK 160
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958789929 161 EDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 197
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-189 3.22e-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: 48.13  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   52 LDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHG--DSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQA 129
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789929  130 SVADAEQRGELALKDAYTKRADLETALQK---AKEDLARLMRDYQELMNVKLALDVEIATYRK 189
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRS 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-192 1.70e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929    5 ELEAKMESLKDEINFMrvlyEAELSQMQTHVSDTSVVLSMDNNRnLDLDGIIAEVRAQYEEIARKSKAEVEswyqikVQQ 84
Cdd:COG4913    621 ELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLDASSDD------LAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   85 LQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGELAL---------------------K 143
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgdaverelrE 769
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958789929  144 DAYTKRADLETALQKAKEDLARLMRDYQEL-MNVKLALDVEIAT---YRKLLE 192
Cdd:COG4913    770 NLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
PRK09039 PRK09039
peptidoglycan -binding protein;
25-165 2.14e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  25 EAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEiARKSKAEVESWYQIKVQQLQMSADQHGD---SLKSTKN 101
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789929 102 EISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGelalKDAYTKRAD----LETALQKAKEDLAR 165
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
1-197 1.20e-81

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 247.91  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   1 MIKVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVESWYQI 80
Cdd:pfam00038 117 LARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  81 KVQQLQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGELALKDAYTKRADLETALQKAK 160
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958789929 161 EDLARLMRDYQELMNVKLALDVEIATYRKLLEGEECR 197
Cdd:pfam00038 277 QEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-189 3.22e-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: 48.13  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   52 LDGIIAEVRAQYEEIARKSKAEVESWYQIKVQQLQMSADQHG--DSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQA 129
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958789929  130 SVADAEQRGELALKDAYTKRADLETALQK---AKEDLARLMRDYQELMNVKLALDVEIATYRK 189
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEElesLEAELEELEAELEELESRLEELEEQLETLRS 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-192 1.70e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929    5 ELEAKMESLKDEINFMrvlyEAELSQMQTHVSDTSVVLSMDNNRnLDLDGIIAEVRAQYEEIARKSKAEVEswyqikVQQ 84
Cdd:COG4913    621 ELEEELAEAEERLEAL----EAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERLDASSDD------LAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   85 LQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGELAL---------------------K 143
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleerfaaalgdaverelrE 769
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958789929  144 DAYTKRADLETALQKAKEDLARLMRDYQEL-MNVKLALDVEIAT---YRKLLE 192
Cdd:COG4913    770 NLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESlpeYLALLD 822
PRK09039 PRK09039
peptidoglycan -binding protein;
25-165 2.14e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  25 EAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEiARKSKAEVESWYQIKVQQLQMSADQHGD---SLKSTKN 101
Cdd:PRK09039   52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958789929 102 EISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRGelalKDAYTKRAD----LETALQKAKEDLAR 165
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
3-176 1.59e-03

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: 39.72  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929   3 KVELEAKMESLKDEINFMRVLYEAELSQMQTHVSDTSVVLSMDNNRNLDLDGIIAEVRAQYEEIARKSKAEVE-----SW 77
Cdd:pfam05557   4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkKK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  78 YQIKVQQLQMSADQH----GDSLKSTKNEISELNRMIQR-------IRSEIENIKKQSQTLQASVADAEQRGE------L 140
Cdd:pfam05557  84 YLEALNKKLNEKESQladaREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQnlekqqS 163
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958789929 141 ALKDAYTKRADLETALQKAKEDLARLMRDYQELMNV 176
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARI 199
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
85-173 5.38e-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: 37.82  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789929  85 LQMSADQHGDSLKSTKNEISELNRMIQRIRSEIENIKKQSQTLQASVADAEQRgelaLKDAYTKRADLETALQKAKEDLA 164
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86

                  ....*....
gi 1958789929 165 RLMRDYQEL 173
Cdd:COG4942    87 ELEKEIAEL 95
 
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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