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Conserved domains on  [gi|1538733338|ref|NP_001354736|]
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F-box and leucine-rich protein 22 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXL22 cd22129
F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also ...
 9-51 1.52e-19

F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also called F-box and leucine-rich repeat protein 22, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). It acts as a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. 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: 438901  Cd Length: 43  Bit Score: 78.70  E-value: 1.52e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1538733338   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:cd22129     1 ITELNRECLLHLFSFLDKDSRRSLSLTCHRLRDVFLDPALWSL 43
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 113-200 1.47e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 44.63  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538733338 113 LRVCDRCPNLASVTLSGCGHVTDDCLARLLRCCPRLRALRLENCARVTNRTLAAVAADGRALQTLHVDFCRN---VSAAG 189
Cdd:cd09293    45 LDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNghlITDVS 124

                          90
                  ....*....|.
gi 1538733338 190 LRRLRAACPRL 200
Cdd:cd09293   125 LSALGKNCTFL 135
 
Name Accession Description Interval E-value
F-box_FBXL22 cd22129
F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also ...
 9-51 1.52e-19

F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also called F-box and leucine-rich repeat protein 22, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). It acts as a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. 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: 438901  Cd Length: 43  Bit Score: 78.70  E-value: 1.52e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1538733338   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:cd22129     1 ITELNRECLLHLFSFLDKDSRRSLSLTCHRLRDVFLDPALWSL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 113-200 1.47e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 44.63  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538733338 113 LRVCDRCPNLASVTLSGCGHVTDDCLARLLRCCPRLRALRLENCARVTNRTLAAVAADGRALQTLHVDFCRN---VSAAG 189
Cdd:cd09293    45 LDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNghlITDVS 124

                          90
                  ....*....|.
gi 1538733338 190 LRRLRAACPRL 200
Cdd:cd09293   125 LSALGKNCTFL 135
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 9-49 8.76e-04

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 35.92  E-value: 8.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1538733338   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALW 49
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLW 41
 
Name Accession Description Interval E-value
F-box_FBXL22 cd22129
F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also ...
 9-51 1.52e-19

F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also called F-box and leucine-rich repeat protein 22, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). It acts as a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. 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: 438901  Cd Length: 43  Bit Score: 78.70  E-value: 1.52e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1538733338   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:cd22129     1 ITELNRECLLHLFSFLDKDSRRSLSLTCHRLRDVFLDPALWSL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 113-200 1.47e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 44.63  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538733338 113 LRVCDRCPNLASVTLSGCGHVTDDCLARLLRCCPRLRALRLENCARVTNRTLAAVAADGRALQTLHVDFCRN---VSAAG 189
Cdd:cd09293    45 LDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRNghlITDVS 124

                          90
                  ....*....|.
gi 1538733338 190 LRRLRAACPRL 200
Cdd:cd09293   125 LSALGKNCTFL 135
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 119-200 3.74e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 43.47  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538733338 119 CPNLASVTLSGCgHVTDDCLARL-LRCCPRLRALRLENCARVTNRTLAAVaadgralqtLHVDFCRNVSAAGLRRlraaC 197
Cdd:cd09293   132 CTFLQTVGFAGC-DVTDKGVWELaSGCSKSLERLSLNNCRNLTDQSIPAI---------LASNYFPNLSVLEFRG----C 197


                  ...
gi 1538733338 198 PRL 200
Cdd:cd09293   198 PLI 200
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 9-49 8.76e-04

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 35.92  E-value: 8.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1538733338   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALW 49
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLW 41
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 12-55 1.68e-03

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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: 438889  Cd Length: 47  Bit Score: 35.29  E-value: 1.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1538733338  12 LNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLHFR 55
Cdd:cd22117     4 LPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNLQ 47
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
 15-53 5.40e-03

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). 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: 438910  Cd Length: 45  Bit Score: 33.84  E-value: 5.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1538733338  15 ECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLH 53
Cdd:cd22138     7 ECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTVD 45
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 100-151 5.59e-03

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 37.36  E-value: 5.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1538733338 100 ICSRHESLVNDFLLRVCDRCPNLASVTLSGCgHVTDDCLARLLRCC-PRLRAL 151
Cdd:cd23951   262 VCANGNSPIDEELIRIAKNCKQLSSLGLGEC-EVSCSALVEFAKLCgPRLTEL 313
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 118-163 6.68e-03

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 36.54  E-value: 6.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1538733338 118 RCPNLASVTLSGCGHVTDDCLARLLR--CCPRLRALRLENCARVTNRT 163
Cdd:cd09293   157 CSKSLERLSLNNCRNLTDQSIPAILAsnYFPNLSVLEFRGCPLITDFS 204
 
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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