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Conserved domains on  [gi|688508333|gb|AIQ84921|]
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caseinolytic protease C, partial (apicoplast) [Haemoproteus tartakovskyi]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClpA super family cl33938
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1-156 1.39e-70

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


The actual alignment was detected with superfamily member COG0542:

Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 228.04  E-value: 1.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:COG0542  619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688508333  81 SNLGcprtynNYLYNKNYLSTLDLQDIQKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQKL 156
Cdd:COG0542  699 SNIG------SELILDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRL 768
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1-156 1.39e-70

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 228.04  E-value: 1.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:COG0542  619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688508333  81 SNLGcprtynNYLYNKNYLSTLDLQDIQKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQKL 156
Cdd:COG0542  699 SNIG------SELILDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRL 768
clpC CHL00095
Clp protease ATP binding subunit
1-156 1.39e-62

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 206.45  E-value: 1.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:CHL00095 579 MEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMT 658
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333  81 SNLGCPRTYNNYLYNKNYLSTLDLQD-----IQKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQK 155
Cdd:CHL00095 659 SNLGSKVIETNSGGLGFELSENQLSEkqykrLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKR 738

                 .
gi 688508333 156 L 156
Cdd:CHL00095 739 L 739
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
1-137 3.52e-61

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 202.88  E-value: 3.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333    1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:TIGR03346 634 MEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMT 713
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688508333   81 SNLGCPRTYNNYLYNknylstlDLQDIQKQILHAINQYFKPELLNRLTNILIFNPLD 137
Cdd:TIGR03346 714 SNLGSDFIQELAGGD-------DYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLG 763
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
1-130 8.14e-54

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 168.53  E-value: 8.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333    1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:pfam07724  43 MEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMT 122
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 688508333   81 SNLGcprtYNNYLYNKNYLSTLDLQDIQKQILHAINQYFKPELLNRLTNI 130
Cdd:pfam07724 123 GNFG----SEKISDASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
1-133 1.65e-49

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 157.72  E-value: 1.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:cd19499   81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508333  81 SNlgcprtynnylynknylstldlqdiqkqilhainqYFKPELLNRLTNILIF 133
Cdd:cd19499  161 SN-----------------------------------HFRPEFLNRIDEIVVF 178
 
Name Accession Description Interval E-value
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1-156 1.39e-70

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 228.04  E-value: 1.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:COG0542  619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688508333  81 SNLGcprtynNYLYNKNYLSTLDLQDIQKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQKL 156
Cdd:COG0542  699 SNIG------SELILDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRL 768
clpC CHL00095
Clp protease ATP binding subunit
1-156 1.39e-62

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 206.45  E-value: 1.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:CHL00095 579 MEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMT 658
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333  81 SNLGCPRTYNNYLYNKNYLSTLDLQD-----IQKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQK 155
Cdd:CHL00095 659 SNLGSKVIETNSGGLGFELSENQLSEkqykrLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKR 738

                 .
gi 688508333 156 L 156
Cdd:CHL00095 739 L 739
chaperone_ClpB TIGR03346
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ...
1-137 3.52e-61

ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 274529 [Multi-domain]  Cd Length: 850  Bit Score: 202.88  E-value: 3.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333    1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:TIGR03346 634 MEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMT 713
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 688508333   81 SNLGCPRTYNNYLYNknylstlDLQDIQKQILHAINQYFKPELLNRLTNILIFNPLD 137
Cdd:TIGR03346 714 SNLGSDFIQELAGGD-------DYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLG 763
ClpA TIGR02639
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ...
1-156 3.51e-56

ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274241 [Multi-domain]  Cd Length: 730  Bit Score: 187.92  E-value: 3.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333    1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:TIGR02639 520 MEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMT 599
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688508333   81 SNLGCPRTYNNYLYNKNYLSTldlqdiqKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQKL 156
Cdd:TIGR02639 600 SNAGASEMSKPPIGFGGENRE-------SKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQL 668
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
1-130 8.14e-54

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 168.53  E-value: 8.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333    1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:pfam07724  43 MEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLIDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMT 122
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 688508333   81 SNLGcprtYNNYLYNKNYLSTLDLQDIQKQILHAINQYFKPELLNRLTNI 130
Cdd:pfam07724 123 GNFG----SEKISDASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
1-133 1.65e-49

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 157.72  E-value: 1.65e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:cd19499   81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 688508333  81 SNlgcprtynnylynknylstldlqdiqkqilhainqYFKPELLNRLTNILIF 133
Cdd:cd19499  161 SN-----------------------------------HFRPEFLNRIDEIVVF 178
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
1-136 5.26e-48

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 166.17  E-value: 5.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:PRK10865 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 688508333  81 SNLGcprtynnYLYNKNYLSTLDLQDIQKQILHAINQYFKPELLNRLTNILIFNPL 136
Cdd:PRK10865 718 SNLG-------SDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPL 766
VI_ClpV1 TIGR03345
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ...
2-146 4.39e-45

type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274528 [Multi-domain]  Cd Length: 852  Bit Score: 158.18  E-value: 4.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333    2 EKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLTS 81
Cdd:TIGR03345 637 EAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTS 716
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688508333   82 NLGCPRTYNNYLYNKNYLSTLDLQDIqkqILHAINQYFKPELLNRLTnILIFNPLDIQTLLLICD 146
Cdd:TIGR03345 717 NAGSDLIMALCADPETAPDPEALLEA---LRPELLKVFKPAFLGRMT-VIPYLPLDDDVLAAIVR 777
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
1-156 5.29e-45

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 157.31  E-value: 5.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688508333   1 MEKHSLSRLIGSPPGYIGYNEGGQLTKQVYNKPYSVILFDEIEKAHSDIYNILLQILDEGRLTDSTGQIIDFTNTIILLT 80
Cdd:PRK11034 525 MERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMT 604
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688508333  81 SNLGCPRTYNNYLynknylsTLDLQDIQKQILHAINQYFKPELLNRLTNILIFNPLDIQTLLLICDKFINEFKQKL 156
Cdd:PRK11034 605 TNAGVRETERKSI-------GLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQL 673
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
36-82 1.12e-05

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 43.05  E-value: 1.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 688508333   36 VILFDEIEKAHSDIYNILLQILDEGRL-TDSTGQIIDF--TNTIILLTSN 82
Cdd:pfam07728  69 IAVLDEINRANPDVLNSLLSLLDERRLlLPDGGELVKAapDGFRLIATMN 118
 
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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