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Conserved domains on  [gi|578814031|ref|XP_006715961|]
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F-box and leucine-rich repeat protein 13 isoform X11 [Homo sapiens]

Protein Classification

F-box/LRR-repeat protein( domain architecture ID 1903223)

F-box/LRR-repeat protein functions as the substrate-recognition component of a SCF (Skp1-Cullin-F-box protein) ubiquitin-protein ligase that is involved in ubiquitin-dependent degradation

CATH:  1.20.1280.50
Gene Ontology:  GO:0019005|GO:0005515|GO:0006511|GO:0016567
PubMed:  31898225|11178263|14747988|7583641|11751054|10581972
SCOP:  4001927

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 288-496 1.50e-19

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: 87.77  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 288 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 365
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 366 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 444
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578814031 445 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 496
Cdd:cd09293  148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 71-256 4.74e-13

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: 68.89  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031  71 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 149
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 150 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 223
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578814031 224 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 256
Cdd:cd09293  186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 15-45 3.06e-10

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 cd22124:

Pssm-ID: 459239  Cd Length: 42  Bit Score: 55.42  E-value: 3.06e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578814031  15 IFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 45
Cdd:cd22124   12 IFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 288-496 1.50e-19

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: 87.77  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 288 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 365
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 366 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 444
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578814031 445 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 496
Cdd:cd09293  148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 71-256 4.74e-13

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: 68.89  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031  71 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 149
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 150 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 223
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578814031 224 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 256
Cdd:cd09293  186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 15-45 3.06e-10

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. 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: 438896  Cd Length: 42  Bit Score: 55.42  E-value: 3.06e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578814031  15 IFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 45
Cdd:cd22124   12 IFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-397 6.96e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.31  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031   1 MKGRLITIILLVTSIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGC 80
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031  81 LLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhisegCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftd 160
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPEELANLTNL---------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 161 kglQYLNLGN-----------GCHKLIYLDLSGCtQISVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITS 229
Cdd:COG4886  139 ---KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QLTD-----LPEELGNLTNLKELD---LSNN----------QITD 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 230 LvftgAPHISDCTfralsacKLRKIRFEGNKrVTDASFKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLAN 309
Cdd:COG4886  197 L----PEPLGNLT-------NLEELDLSGNQ-LTDLPEPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSN 259

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 310 CvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASVMKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGT 389
Cdd:COG4886  260 N-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332


                 ....*...
gi 578814031 390 DISNEGLN 397
Cdd:COG4886  333 LLVTLTTL 340
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 288-496 1.50e-19

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: 87.77  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 288 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 365
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 366 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 444
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578814031 445 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 496
Cdd:cd09293  148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 381-521 1.02e-17

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: 82.38  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 381 LVSIDLSGTDISNEGLNVLSRHKKLKELSVSECYRITDDGIQAFCKSSLILEHLDVSYCSQLSDMIIKALAIYCINLTSL 460
Cdd:cd09293   30 LEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTI 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578814031 461 SI---AGCPKITDSAMEMLSAKCHYLHILDISGCvLLTDQILEDLQIGC-KQLRILKMQYCTNIS 521
Cdd:cd09293  110 NLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLT 173
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 224-470 3.37e-15

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: 75.06  E-value: 3.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 224 CSRITSLVFTGAPhISDCTFRALSAC-KLRKIRFEGNKRVTDASFKFIDKNYPNLSHIYMADCKGITDSSLRSLSP-LKQ 301
Cdd:cd09293   27 HSGLEWLELYMCP-ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 302 LTVLNLancvrigdmGLKQfldgpasmrirelnlsNCVRLSDASVMKLSERCPNLNylslrncehltaqgigyivnifsl 381
Cdd:cd09293  106 LQTINL---------GRHR----------------NGHLITDVSLSALGKNCTFLQ------------------------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 382 vSIDLSGTDISNEGLNVLSRH--KKLKELSVSECYRITDDGIqafcksSLILEHLdvsycsqlsdmiikalaiYCINLTS 459
Cdd:cd09293  137 -TVGFAGCDVTDKGVWELASGcsKSLERLSLNNCRNLTDQSI------PAILASN------------------YFPNLSV 191

                        250
                 ....*....|.
gi 578814031 460 LSIAGCPKITD 470
Cdd:cd09293  192 LEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 71-256 4.74e-13

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: 68.89  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031  71 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 149
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 150 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 223
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578814031 224 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 256
Cdd:cd09293  186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 197-345 2.40e-10

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: 60.80  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 197 SCTGIMHLTINDMPTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA-CKLRKI----RFEGNKRVTDASFKFID 271
Cdd:cd09293   50 NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTinlgRHRNGHLITDVSLSALG 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578814031 272 KNYPNLSHIYMADCKgITDSSLRSLSPL--KQLTVLNLANCVRIGDMGLKQFLDGPASMRIRELNLSNCVRLSDAS 345
Cdd:cd09293  130 KNCTFLQTVGFAGCD-VTDKGVWELASGcsKSLERLSLNNCRNLTDQSIPAILASNYFPNLSVLEFRGCPLITDFS 204
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 15-45 3.06e-10

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. 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: 438896  Cd Length: 42  Bit Score: 55.42  E-value: 3.06e-10
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578814031  15 IFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 45
Cdd:cd22124   12 IFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 125-362 2.85e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.19  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 125 LNLSNTTITNRTMRLLPRHFHNLQNLS-LAYCRRFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRYIAN 196
Cdd:cd00116   28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 197 SCT-GIMHLTINDM-PTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA----CKLRKIRFeGNKRVTDASFKFI 270
Cdd:cd00116  107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAlranRDLKELNL-ANNGIGDAGIRAL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 271 D---KNYPNLSHIYMADCkGITDSSLRSLS----PLKQLTVLNLANCVrIGDMGLKQFLDG--PASMRIRELNLSNCvRL 341
Cdd:cd00116  186 AeglKANCNLEVLDLNNN-GLTDEGASALAetlaSLKSLEVLNLGDNN-LTDAGAAALASAllSPNISLLTLSLSCN-DI 262

                        250       260
                 ....*....|....*....|....
gi 578814031 342 SDASVMKLSERCPN---LNYLSLR 362
Cdd:cd00116  263 TDDGAKDLAEVLAEkesLLELDLR 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-397 6.96e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.31  E-value: 6.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031   1 MKGRLITIILLVTSIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGC 80
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031  81 LLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhisegCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftd 160
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPEELANLTNL---------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 161 kglQYLNLGN-----------GCHKLIYLDLSGCtQISVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITS 229
Cdd:COG4886  139 ---KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QLTD-----LPEELGNLTNLKELD---LSNN----------QITD 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 230 LvftgAPHISDCTfralsacKLRKIRFEGNKrVTDASFKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLAN 309
Cdd:COG4886  197 L----PEPLGNLT-------NLEELDLSGNQ-LTDLPEPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSN 259

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578814031 310 CvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASVMKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGT 389
Cdd:COG4886  260 N-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332


                 ....*...
gi 578814031 390 DISNEGLN 397
Cdd:COG4886  333 LLVTLTTL 340
 
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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