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Conserved domains on  [gi|18390613|ref|NP_563759|]
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SKP1/ASK-interacting protein 16 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 314-409 6.89e-31

ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity.


:

Pssm-ID: 461283  Cd Length: 87  Bit Score: 113.71  E-value: 6.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613   314 SNLRDQPPAYWYAYSIRMSLMPEgcilngthhSSCQLYWRHWVIRADNEVIDNVNGEAVIGKYPLLQAGeEEFVYESCSS 393
Cdd:pfam04379   2 EQSSPEEGRYVFAYTIRIENLGD---------SSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVLAPG-ESFEYTSGCP 71

                          90
                  ....*....|....*.
gi 18390613   394 FPTTAGSIDGSFTFVP 409
Cdd:pfam04379  72 LETPSGSMEGSYTMVR 87
SMI1 super family cl44049
Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane ...
 88-183 2.42e-11

Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG4282:

Pssm-ID: 443423  Cd Length: 188  Bit Score: 62.36  E-value: 2.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613  88 RVRLCWDNLKQWLTLNFPEAKATLRKGVTEDDLQEFETSLKVKLPLPTRLLYRFVDGQelsspnGLDGSLGLIGGYSays 167
Cdd:COG4282   3 SVAESWERIEAWLAEHAPDLLAALRPGASEADIAALEAALGVELPEDLRALYRIHNGQ------GDDALPGLFGNYR--- 73

                        90
                ....*....|....*.
gi 18390613 168 hdvnvyLLPLKEVMRE 183
Cdd:COG4282  74 ------LLSLEEILDE 83
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 8-47 2.06e-04

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


The actual alignment was detected with superfamily member cd22151:

Pssm-ID: 459239  Cd Length: 44  Bit Score: 38.84  E-value: 2.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18390613   8 DLVLHIVLSKIGPENTARVACVSKRLKVSASEESLWSIFC 47
Cdd:cd22151   5 DDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44
 
Name Accession Description Interval E-value
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 314-409 6.89e-31

ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity.


Pssm-ID: 461283  Cd Length: 87  Bit Score: 113.71  E-value: 6.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613   314 SNLRDQPPAYWYAYSIRMSLMPEgcilngthhSSCQLYWRHWVIRADNEVIDNVNGEAVIGKYPLLQAGeEEFVYESCSS 393
Cdd:pfam04379   2 EQSSPEEGRYVFAYTIRIENLGD---------SSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVLAPG-ESFEYTSGCP 71

                          90
                  ....*....|....*.
gi 18390613   394 FPTTAGSIDGSFTFVP 409
Cdd:pfam04379  72 LETPSGSMEGSYTMVR 87
apaG PRK05461
CO2+/MG2+ efflux protein ApaG; Reviewed
 293-432 8.04e-18

CO2+/MG2+ efflux protein ApaG; Reviewed


Pssm-ID: 180098  Cd Length: 127  Bit Score: 79.04  E-value: 8.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613  293 CSVSVTNGVQVRASSVFIPEISNLRDQppAYWYAYSIRmslmpegcILN-GTHhsSCQLYWRHWVIRADNEVIDNVNGEA 371
Cdd:PRK05461   1 MYSAVTYGIEVSVQPRYLEEQSDPEEG--RYVFAYTIT--------IENlGRV--PVQLLSRHWLITDANGRVQEVRGEG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390613  372 VIGKYPLLQAGeEEFVYESCSSFPTTAGSIDGSFTFVpgslrDPKGSQFEVKVVEFPLELP 432
Cdd:PRK05461  69 VVGEQPVLAPG-ESFEYTSGAVLETPSGTMQGHYQMV-----DEDGERFEVPIPPFRLAVP 123
SMI1 COG4282
Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane ...
 88-183 2.42e-11

Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443423  Cd Length: 188  Bit Score: 62.36  E-value: 2.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613  88 RVRLCWDNLKQWLTLNFPEAKATLRKGVTEDDLQEFETSLKVKLPLPTRLLYRFVDGQelsspnGLDGSLGLIGGYSays 167
Cdd:COG4282   3 SVAESWERIEAWLAEHAPDLLAALRPGASEADIAALEAALGVELPEDLRALYRIHNGQ------GDDALPGLFGNYR--- 73

                        90
                ....*....|....*.
gi 18390613 168 hdvnvyLLPLKEVMRE 183
Cdd:COG4282  74 ------LLSLEEILDE 83
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 8-47 2.06e-04

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438922  Cd Length: 44  Bit Score: 38.84  E-value: 2.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18390613   8 DLVLHIVLSKIGPENTARVACVSKRLKVSASEESLWSIFC 47
Cdd:cd22151   5 DDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44
 
Name Accession Description Interval E-value
DUF525 pfam04379
ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins ...
 314-409 6.89e-31

ApaG domain; The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity.


Pssm-ID: 461283  Cd Length: 87  Bit Score: 113.71  E-value: 6.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613   314 SNLRDQPPAYWYAYSIRMSLMPEgcilngthhSSCQLYWRHWVIRADNEVIDNVNGEAVIGKYPLLQAGeEEFVYESCSS 393
Cdd:pfam04379   2 EQSSPEEGRYVFAYTIRIENLGD---------SSVQLLSRHWIITDANGKVEEVRGEGVVGEQPVLAPG-ESFEYTSGCP 71

                          90
                  ....*....|....*.
gi 18390613   394 FPTTAGSIDGSFTFVP 409
Cdd:pfam04379  72 LETPSGSMEGSYTMVR 87
apaG PRK05461
CO2+/MG2+ efflux protein ApaG; Reviewed
 293-432 8.04e-18

CO2+/MG2+ efflux protein ApaG; Reviewed


Pssm-ID: 180098  Cd Length: 127  Bit Score: 79.04  E-value: 8.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613  293 CSVSVTNGVQVRASSVFIPEISNLRDQppAYWYAYSIRmslmpegcILN-GTHhsSCQLYWRHWVIRADNEVIDNVNGEA 371
Cdd:PRK05461   1 MYSAVTYGIEVSVQPRYLEEQSDPEEG--RYVFAYTIT--------IENlGRV--PVQLLSRHWLITDANGRVQEVRGEG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390613  372 VIGKYPLLQAGeEEFVYESCSSFPTTAGSIDGSFTFVpgslrDPKGSQFEVKVVEFPLELP 432
Cdd:PRK05461  69 VVGEQPVLAPG-ESFEYTSGAVLETPSGTMQGHYQMV-----DEDGERFEVPIPPFRLAVP 123
SMI1 COG4282
Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane ...
 88-183 2.42e-11

Cell wall assembly regulator SMI1 (Killer toxin-resistance protein 4) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443423  Cd Length: 188  Bit Score: 62.36  E-value: 2.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390613  88 RVRLCWDNLKQWLTLNFPEAKATLRKGVTEDDLQEFETSLKVKLPLPTRLLYRFVDGQelsspnGLDGSLGLIGGYSays 167
Cdd:COG4282   3 SVAESWERIEAWLAEHAPDLLAALRPGASEADIAALEAALGVELPEDLRALYRIHNGQ------GDDALPGLFGNYR--- 73

                        90
                ....*....|....*.
gi 18390613 168 hdvnvyLLPLKEVMRE 183
Cdd:COG4282  74 ------LLSLEEILDE 83
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 8-47 2.06e-04

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438922  Cd Length: 44  Bit Score: 38.84  E-value: 2.06e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18390613   8 DLVLHIVLSKIGPENTARVACVSKRLKVSASEESLWSIFC 47
Cdd:cd22151   5 DDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44
 
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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