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Conserved domains on  [gi|2462613053|ref|XP_054213565|]
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F-box and leucine-rich repeat protein 13 isoform X16 [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 ...
 288-468 7.76e-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: 85.46  E-value: 7.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 288 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 365
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 366 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 436
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462613053 437 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 468
Cdd:cd09293   169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 71-256 4.39e-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: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053  71 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 149
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 150 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 223
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462613053 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 3.40e-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: 3.40e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462613053  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 ...
 288-468 7.76e-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: 85.46  E-value: 7.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 288 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 365
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 366 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 436
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462613053 437 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 468
Cdd:cd09293   169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 71-256 4.39e-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: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053  71 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 149
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 150 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 223
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462613053 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 3.40e-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: 3.40e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462613053  15 IFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 45
Cdd:cd22124    12 IFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-394 7.09e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.31  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053   1 MKGRLITIILLVTSIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGC 80
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053  81 LLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhisegCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftd 160
Cdd:COG4886    83 SLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPEELANLTNL---------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 161 kglQYLNLGN-----------GCHKLIYLDLSGCtQISVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITS 229
Cdd:COG4886   139 ---KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QLTD-----LPEELGNLTNLKELD---LSNN----------QITD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 230 LvftgAPHISDCTfralsacKLRKIRFEGNKrVTDASFKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLAN 309
Cdd:COG4886   197 L----PEPLGNLT-------NLEELDLSGNQ-LTDLPEPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSN 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 310 CvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASVMKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGT 389
Cdd:COG4886   260 N-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332


                  ....*
gi 2462613053 390 DISNE 394
Cdd:COG4886   333 LLVTL 337
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 288-468 7.76e-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: 85.46  E-value: 7.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 288 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 365
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 366 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 436
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2462613053 437 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 468
Cdd:cd09293   169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 71-256 4.39e-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: 4.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053  71 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 149
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 150 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 223
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462613053 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 2.23e-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: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 197 SCTGIMHLTINDMPTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA-CKLRKI----RFEGNKRVTDASFKFID 271
Cdd:cd09293    50 NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTinlgRHRNGHLITDVSLSALG 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462613053 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 3.40e-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: 3.40e-10
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462613053  15 IFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 45
Cdd:cd22124    12 IFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 403-484 7.89e-08

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: 53.10  E-value: 7.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 403 LEHLDVsYCSQLSDMIIKALaIYCINLTSLSIAGCPKITDSAMEMLSAKCHYLHILDISGCVLLTDQILEDLQIGCKQLR 482
Cdd:cd09293    30 LEWLEL-YMCPISDPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQ 107


                  ..
gi 2462613053 483 IL 484
Cdd:cd09293   108 TI 109
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 125-362 2.12e-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: 46.58  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 125 LNLSNTTITNRTMRLLPRHFHNLQNLS-LAYCRRFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRYIAN 196
Cdd:cd00116    28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 197 SCT-GIMHLTINDM-PTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA----CKLRKIRFeGNKRVTDASFKFI 270
Cdd:cd00116   107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAlranRDLKELNL-ANNGIGDAGIRAL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 271 D---KNYPNLSHIYMADCkGITDSSLRSLS----PLKQLTVLNLANCVrIGDMGLKQFLDG--PASMRIRELNLSNCvRL 341
Cdd:cd00116   186 AeglKANCNLEVLDLNNN-GLTDEGASALAetlaSLKSLEVLNLGDNN-LTDAGAAALASAllSPNISLLTLSLSCN-DI 262

                         250       260
                  ....*....|....*....|....
gi 2462613053 342 SDASVMKLSERCPN---LNYLSLR 362
Cdd:cd00116   263 TDDGAKDLAEVLAEkesLLELDLR 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-394 7.09e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.31  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053   1 MKGRLITIILLVTSIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGC 80
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053  81 LLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhisegCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftd 160
Cdd:COG4886    83 SLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPEELANLTNL---------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 161 kglQYLNLGN-----------GCHKLIYLDLSGCtQISVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITS 229
Cdd:COG4886   139 ---KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QLTD-----LPEELGNLTNLKELD---LSNN----------QITD 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 230 LvftgAPHISDCTfralsacKLRKIRFEGNKrVTDASFKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLAN 309
Cdd:COG4886   197 L----PEPLGNLT-------NLEELDLSGNQ-LTDLPEPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSN 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 310 CvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASVMKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGT 389
Cdd:COG4886   260 N-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332


                  ....*
gi 2462613053 390 DISNE 394
Cdd:COG4886   333 LLVTL 337
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 412-493 9.00e-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: 38.08  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613053 412 SQLSDMIIKAL-AIYCINLTSLSIAGCPKItDSAMEMLSAkCHYLHILDISGCVLLTDQILEDLQIGCKQLRILKMQYCT 490
Cdd:cd09293    12 GQITQSNISQLlRILHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89


                  ...
gi 2462613053 491 NIS 493
Cdd:cd09293    90 NIT 92
 
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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