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Conserved domains on  [gi|18411999|ref|NP_567113|]
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SKP1-like 21 [Arabidopsis thaliana]

Protein Classification

SKP1-like protein( domain architecture ID 10649839)

SKP1-like protein is a component of E3 ubiquitin ligase SCF complex involved in ubiquitination and subsequent proteasomal degradation of target proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Skp1 smart00512
Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle ...
15-116 3.63e-24

Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle progression) and elongin C (subunit of RNA polymerase II transcription factor SIII) homologues.


:

Pssm-ID: 214704  Cd Length: 104  Bit Score: 95.05  E-value: 3.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999     15 KSYIWLETADGSIQQVEQEVAMFCPMICQEVIQKGVGSSKNYAISLPQrVNPAMLSLIFDYCRFHQVPGRSNKE---RKV 91
Cdd:smart00512   1 SKYIKLISSDGEVFEVEREVARQSKTIKAMIEDLGVDDENNNPIPLPN-VTSKILSKVIEYCEHHVDDPPSVADkddIPT 79
                           90       100
                   ....*....|....*....|....*
gi 18411999     92 YDEKFIRMDTKRLCELTSAADSLQL 116
Cdd:smart00512  80 WDAEFLKIDQETLFELILAANYLDI 104
Skp1 pfam01466
Skp1 family, dimerization domain;
117-156 1.49e-10

Skp1 family, dimerization domain;


:

Pssm-ID: 460222  Cd Length: 48  Bit Score: 55.97  E-value: 1.49e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18411999   117 KPLVDLTSRALARIIEGKTPEEIREIFHLPDDLTEEEKLE 156
Cdd:pfam01466   1 KGLLDLTCKTVADMIKGKTPEEIREIFNIENDFTPEEEEE 40
serpin super family cl38926
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ...
132-192 3.59e-03

SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


The actual alignment was detected with superfamily member cd19955:

Pssm-ID: 476815 [Multi-domain]  Cd Length: 361  Bit Score: 38.79  E-value: 3.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411999 132 EGKTPEEIREIFHLPDDlteEEKLE-------PLKNTMDDPRIRLLNRLYAKKRKELKEREKLKSVEV 192
Cdd:cd19955  40 KGETAEEIRTVLHLPSS---KEKIEeayksllPKLKNSEGYTLHTANKIYVKDKFKINPDFKKIAKDI 104
 
Name Accession Description Interval E-value
Skp1 smart00512
Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle ...
15-116 3.63e-24

Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle progression) and elongin C (subunit of RNA polymerase II transcription factor SIII) homologues.


Pssm-ID: 214704  Cd Length: 104  Bit Score: 95.05  E-value: 3.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999     15 KSYIWLETADGSIQQVEQEVAMFCPMICQEVIQKGVGSSKNYAISLPQrVNPAMLSLIFDYCRFHQVPGRSNKE---RKV 91
Cdd:smart00512   1 SKYIKLISSDGEVFEVEREVARQSKTIKAMIEDLGVDDENNNPIPLPN-VTSKILSKVIEYCEHHVDDPPSVADkddIPT 79
                           90       100
                   ....*....|....*....|....*
gi 18411999     92 YDEKFIRMDTKRLCELTSAADSLQL 116
Cdd:smart00512  80 WDAEFLKIDQETLFELILAANYLDI 104
SKP1 COG5201
SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, ...
16-153 3.57e-14

SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227528 [Multi-domain]  Cd Length: 158  Bit Score: 69.20  E-value: 3.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999  16 SYIWLETADGSIQQVEQEVAMFCPMICQEVIQKGvgsSKNYAISLPqRVNPAMLSLIFDYCRFHQVPG---------RSN 86
Cdd:COG5201   2 SMIELESIDGEIFRVDENIAERSILIKNMLCDST---ACNYPIPAP-NVRSSVLMKVQEWMEHHTSSLsedendleiRKS 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411999  87 KERKVYDEKFIRMDTKRLCELTSAADSLQLKPLVDLTSRALARIIEGKTPEEIREIFHLPDDLTEEE 153
Cdd:COG5201  78 KPSDFWDRFFMEVDQEMLLEICLAANYLEIKPLLDLGCKIVAEMIRGKSPEEIRETFNIENDFTPEE 144
Skp1 pfam01466
Skp1 family, dimerization domain;
117-156 1.49e-10

Skp1 family, dimerization domain;


Pssm-ID: 460222  Cd Length: 48  Bit Score: 55.97  E-value: 1.49e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18411999   117 KPLVDLTSRALARIIEGKTPEEIREIFHLPDDLTEEEKLE 156
Cdd:pfam01466   1 KGLLDLTCKTVADMIKGKTPEEIREIFNIENDFTPEEEEE 40
BTB_POZ_SKP1 cd18322
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
17-131 1.04e-07

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in S-phase kinase-associated protein 1 (SKP1) and similar proteins; SKP1 is also called cyclin-A/CDK2-associated protein p19 (p19A), organ of Corti protein 2 (OCP-2), organ of Corti protein II (OCP-II), RNA polymerase II elongation factor-like protein, transcription elongation factor B polypeptide 1-like, or p19skp1. It is an essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 serves as an adaptor protein that links the F-box protein to CUL1. SKP1 and CUL1 are invariant components of all SCF complexes, while F-box proteins are variable substrate binding modules that determine specificity. SKP1 belongs to the BTB/POZ domain family; the domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349631  Cd Length: 120  Bit Score: 49.90  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999  17 YIWLETADGSIQQVEQEVAMFCPMICQEVIQKGVgssKNYAISLPQrVNPAMLSLIFDYCRFHQV---------PGRSNK 87
Cdd:cd18322   1 KIKLQSSDGEIFEVDEEVARQSVTIKNMLEDLGY---DDDPIPLPN-VTSKILKKVIEWCEHHKDdpppeidldSEKRTD 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18411999  88 ERKVYDEKFIRMDTKRLCELTSAADSLQLKPLVDLTSRALARII 131
Cdd:cd18322  77 DIPEWDAEFLKVDQDTLFELILAANYLDIKGLLDLTCKTVANMI 120
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
132-192 3.59e-03

insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381071 [Multi-domain]  Cd Length: 361  Bit Score: 38.79  E-value: 3.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411999 132 EGKTPEEIREIFHLPDDlteEEKLE-------PLKNTMDDPRIRLLNRLYAKKRKELKEREKLKSVEV 192
Cdd:cd19955  40 KGETAEEIRTVLHLPSS---KEKIEeayksllPKLKNSEGYTLHTANKIYVKDKFKINPDFKKIAKDI 104
 
Name Accession Description Interval E-value
Skp1 smart00512
Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle ...
15-116 3.63e-24

Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle progression) and elongin C (subunit of RNA polymerase II transcription factor SIII) homologues.


Pssm-ID: 214704  Cd Length: 104  Bit Score: 95.05  E-value: 3.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999     15 KSYIWLETADGSIQQVEQEVAMFCPMICQEVIQKGVGSSKNYAISLPQrVNPAMLSLIFDYCRFHQVPGRSNKE---RKV 91
Cdd:smart00512   1 SKYIKLISSDGEVFEVEREVARQSKTIKAMIEDLGVDDENNNPIPLPN-VTSKILSKVIEYCEHHVDDPPSVADkddIPT 79
                           90       100
                   ....*....|....*....|....*
gi 18411999     92 YDEKFIRMDTKRLCELTSAADSLQL 116
Cdd:smart00512  80 WDAEFLKIDQETLFELILAANYLDI 104
SKP1 COG5201
SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, ...
16-153 3.57e-14

SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227528 [Multi-domain]  Cd Length: 158  Bit Score: 69.20  E-value: 3.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999  16 SYIWLETADGSIQQVEQEVAMFCPMICQEVIQKGvgsSKNYAISLPqRVNPAMLSLIFDYCRFHQVPG---------RSN 86
Cdd:COG5201   2 SMIELESIDGEIFRVDENIAERSILIKNMLCDST---ACNYPIPAP-NVRSSVLMKVQEWMEHHTSSLsedendleiRKS 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411999  87 KERKVYDEKFIRMDTKRLCELTSAADSLQLKPLVDLTSRALARIIEGKTPEEIREIFHLPDDLTEEE 153
Cdd:COG5201  78 KPSDFWDRFFMEVDQEMLLEICLAANYLEIKPLLDLGCKIVAEMIRGKSPEEIRETFNIENDFTPEE 144
Skp1 pfam01466
Skp1 family, dimerization domain;
117-156 1.49e-10

Skp1 family, dimerization domain;


Pssm-ID: 460222  Cd Length: 48  Bit Score: 55.97  E-value: 1.49e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 18411999   117 KPLVDLTSRALARIIEGKTPEEIREIFHLPDDLTEEEKLE 156
Cdd:pfam01466   1 KGLLDLTCKTVADMIKGKTPEEIREIFNIENDFTPEEEEE 40
BTB_POZ_SKP1 cd18322
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
17-131 1.04e-07

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in S-phase kinase-associated protein 1 (SKP1) and similar proteins; SKP1 is also called cyclin-A/CDK2-associated protein p19 (p19A), organ of Corti protein 2 (OCP-2), organ of Corti protein II (OCP-II), RNA polymerase II elongation factor-like protein, transcription elongation factor B polypeptide 1-like, or p19skp1. It is an essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 serves as an adaptor protein that links the F-box protein to CUL1. SKP1 and CUL1 are invariant components of all SCF complexes, while F-box proteins are variable substrate binding modules that determine specificity. SKP1 belongs to the BTB/POZ domain family; the domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349631  Cd Length: 120  Bit Score: 49.90  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411999  17 YIWLETADGSIQQVEQEVAMFCPMICQEVIQKGVgssKNYAISLPQrVNPAMLSLIFDYCRFHQV---------PGRSNK 87
Cdd:cd18322   1 KIKLQSSDGEIFEVDEEVARQSVTIKNMLEDLGY---DDDPIPLPN-VTSKILKKVIEWCEHHKDdpppeidldSEKRTD 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18411999  88 ERKVYDEKFIRMDTKRLCELTSAADSLQLKPLVDLTSRALARII 131
Cdd:cd18322  77 DIPEWDAEFLKVDQDTLFELILAANYLDIKGLLDLTCKTVANMI 120
serpin48-like_insects cd19955
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ...
132-192 3.59e-03

insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381071 [Multi-domain]  Cd Length: 361  Bit Score: 38.79  E-value: 3.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411999 132 EGKTPEEIREIFHLPDDlteEEKLE-------PLKNTMDDPRIRLLNRLYAKKRKELKEREKLKSVEV 192
Cdd:cd19955  40 KGETAEEIRTVLHLPSS---KEKIEeayksllPKLKNSEGYTLHTANKIYVKDKFKINPDFKKIAKDI 104
 
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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