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Conserved domains on  [gi|1034654511|ref|XP_016867339|]
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F-box and leucine-rich repeat protein 13 isoform X1 [Homo sapiens]

Protein Classification

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 ...
 526-734 6.98e-20

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: 89.31  E-value: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 526 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 603
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 604 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 682
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034654511 683 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 734
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 242-283 2.12e-16

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: 73.52  E-value: 2.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 309-494 3.02e-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: 70.05  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 309 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 387
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 388 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 461
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034654511 462 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 494
Cdd:cd09293   186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 8-47 7.50e-13

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


:

Pssm-ID: 438546  Cd Length: 43  Bit Score: 63.34  E-value: 7.50e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654511   8 NPRLKNYFKENYIPQ---ALLCGILVTCPEDPLRYLEGMIMVI 47
Cdd:cd22977     1 DPELRKYLRKHKLPDvyeALLTGLAVMCPEDPLRFIEEKLKEL 43
Sfi1 super family cl25835
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 109-221 5.46e-04

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.


The actual alignment was detected with superfamily member pfam08457:

Pssm-ID: 430007 [Multi-domain]  Cd Length: 570  Bit Score: 43.44  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 109 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 187
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034654511 188 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 221
Cdd:pfam08457 379 VQKlekwarDARFYFLATR--TLKKW-------RAATEES 409
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 526-734 6.98e-20

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: 89.31  E-value: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 526 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 603
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 604 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 682
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034654511 683 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 734
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 242-283 2.12e-16

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: 73.52  E-value: 2.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 309-494 3.02e-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: 70.05  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 309 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 387
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 388 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 461
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034654511 462 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 494
Cdd:cd09293   186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 8-47 7.50e-13

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438546  Cd Length: 43  Bit Score: 63.34  E-value: 7.50e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654511   8 NPRLKNYFKENYIPQ---ALLCGILVTCPEDPLRYLEGMIMVI 47
Cdd:cd22977     1 DPELRKYLRKHKLPDvyeALLTGLAVMCPEDPLRFIEEKLKEL 43
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 242-286 8.99e-05

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 40.54  E-value: 8.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 286
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
276-635 2.97e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 276 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 355
Cdd:COG4886    40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 356 gCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftdkglQYLNLGN-----------GCHKLIYLDLSGCtQI 424
Cdd:COG4886   112 -LTNLESLDLSGNQLTD-----LPEELANLTNL-------------KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 425 SVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDAS 504
Cdd:COG4886   172 TD-----LPEELGNLTNLKELD---LSNN----------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 505 FKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASV 584
Cdd:COG4886   222 EPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKL 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034654511 585 MKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGTDISNEGLN 635
Cdd:COG4886   290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTL 340
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 109-221 5.46e-04

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.


Pssm-ID: 430007 [Multi-domain]  Cd Length: 570  Bit Score: 43.44  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 109 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 187
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034654511 188 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 221
Cdd:pfam08457 379 VQKlekwarDARFYFLATR--TLKKW-------RAATEES 409
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
641-665 9.87e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 9.87e-03
                           10        20
                   ....*....|....*....|....*
gi 1034654511  641 KKLKELSVSECYRITDDGIQAFCKS 665
Cdd:smart00367   2 PNLRELDLSGCTNITDEGLQALAKG 26
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 526-734 6.98e-20

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: 89.31  E-value: 6.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 526 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 603
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 604 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 682
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034654511 683 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 734
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 619-759 6.45e-18

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: 83.53  E-value: 6.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 619 LVSIDLSGTDISNEGLNVLSRHKKLKELSVSECYRITDDGIQAFCKSSLILEHLDVSYCSQLSDMIIKALAIYCINLTSL 698
Cdd:cd09293    30 LEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTI 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654511 699 SI---AGCPKITDSAMEMLSAKCHYLHILDISGCvLLTDQILEDLQIGC-KQLRILKMQYCTNIS 759
Cdd:cd09293   110 NLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLT 173
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 242-283 2.12e-16

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: 73.52  E-value: 2.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 283
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 462-708 1.61e-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: 76.60  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 462 CSRITSLVFTGAPhISDCTFRALSAC-KLRKIRFEGNKRVTDASFKFIDKNYPNLSHIYMADCKGITDSSLRSLSP-LKQ 539
Cdd:cd09293    27 HSGLEWLELYMCP-ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 540 LTVLNLancvrigdmGLKQfldgpasmrirelnlsNCVRLSDASVMKLSERCPNLNylslrncehltaqgigyivnifsl 619
Cdd:cd09293   106 LQTINL---------GRHR----------------NGHLITDVSLSALGKNCTFLQ------------------------ 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 620 vSIDLSGTDISNEGLNVLSRH--KKLKELSVSECYRITDDGIqafcksSLILEHLdvsycsqlsdmiikalaiYCINLTS 697
Cdd:cd09293   137 -TVGFAGCDVTDKGVWELASGcsKSLERLSLNNCRNLTDQSI------PAILASN------------------YFPNLSV 191

                         250
                  ....*....|.
gi 1034654511 698 LSIAGCPKITD 708
Cdd:cd09293   192 LEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 309-494 3.02e-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: 70.05  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 309 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 387
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 388 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 461
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034654511 462 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 494
Cdd:cd09293   186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 8-47 7.50e-13

dimerization/docking (D/D) 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 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438546  Cd Length: 43  Bit Score: 63.34  E-value: 7.50e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654511   8 NPRLKNYFKENYIPQ---ALLCGILVTCPEDPLRYLEGMIMVI 47
Cdd:cd22977     1 DPELRKYLRKHKLPDvyeALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 416-583 1.88e-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: 61.57  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 416 LDLSGCtQISVQGFRYIANsCTGIMHLTINDMPTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA-CKLRKI-- 492
Cdd:cd09293    33 LELYMC-PISDPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTin 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 493 --RFEGNKRVTDASFKFIDKNYPNLSHIYMADCKgITDSSLRSLSPL--KQLTVLNLANCVRIGDMGLKQFLDGPASMRI 568
Cdd:cd09293   111 lgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGcsKSLERLSLNNCRNLTDQSIPAILASNYFPNL 189

                         170
                  ....*....|....*
gi 1034654511 569 RELNLSNCVRLSDAS 583
Cdd:cd09293   190 SVLEFRGCPLITDFS 204
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 242-284 5.95e-06

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction 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: 438919  Cd Length: 44  Bit Score: 43.81  E-value: 5.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNA 284
Cdd:cd22148     2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 242-282 2.33e-05

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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: 438890  Cd Length: 41  Bit Score: 41.94  E-value: 2.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 282
Cdd:cd22118     1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 363-600 3.09e-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: 46.96  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 363 LNLSNTTITNRTMRLLPRHFHNLQNLS-LAYCRRFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRYIAN 434
Cdd:cd00116    28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 435 SCT-GIMHLTINDM-PTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA----CKLRKIRFeGNKRVTDASFKFI 508
Cdd:cd00116   107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAlranRDLKELNL-ANNGIGDAGIRAL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 509 D---KNYPNLSHIYMADCkGITDSSLRSLS----PLKQLTVLNLANCVrIGDMGLKQFLDG--PASMRIRELNLSNCvRL 579
Cdd:cd00116   186 AeglKANCNLEVLDLNNN-GLTDEGASALAetlaSLKSLEVLNLGDNN-LTDAGAAALASAllSPNISLLTLSLSCN-DI 262

                         250       260
                  ....*....|....*....|....
gi 1034654511 580 SDASVMKLSERCPN---LNYLSLR 600
Cdd:cd00116   263 TDDGAKDLAEVLAEkesLLELDLR 286
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 242-286 8.99e-05

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 40.54  E-value: 8.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 286
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 242-282 2.38e-04

F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also called F-box and leucine-rich repeat protein 12, or F-box protein FBL12, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the polyubiquitination and proteasomal degradation of calcium/calmodulin dependent protein kinase I (CAMK1) leading to disruption of cyclin D1/CDK4 complex assembly, which results in G1 cell cycle arrest in lung epithelia. It regulates T-cell differentiation in a cell-autonomous manner. 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: 438895  Cd Length: 42  Bit Score: 39.26  E-value: 2.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034654511 242 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 282
Cdd:cd22123     1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
276-635 2.97e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 276 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 355
Cdd:COG4886    40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 356 gCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftdkglQYLNLGN-----------GCHKLIYLDLSGCtQI 424
Cdd:COG4886   112 -LTNLESLDLSGNQLTD-----LPEELANLTNL-------------KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 425 SVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDAS 504
Cdd:COG4886   172 TD-----LPEELGNLTNLKELD---LSNN----------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 505 FKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASV 584
Cdd:COG4886   222 EPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKL 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034654511 585 MKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGTDISNEGLN 635
Cdd:COG4886   290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTL 340
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 243-282 4.44e-04

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. 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: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 38.75  E-value: 4.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1034654511 243 SLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 282
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 109-221 5.46e-04

Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a role in spindle body duplication. They contain binding sites for calmodulin-like proteins called centrins which are present in microtubule-organizing centres.


Pssm-ID: 430007 [Multi-domain]  Cd Length: 570  Bit Score: 43.44  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654511 109 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 187
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034654511 188 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 221
Cdd:pfam08457 379 VQKlekwarDARFYFLATR--TLKKW-------RAATEES 409
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 243-272 2.34e-03

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.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 36.27  E-value: 2.34e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034654511 243 SLLPERAILQIFFYLSLKDVIICGQVNHAW 272
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRW 30
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 241-285 2.84e-03

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. 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: 438906  Cd Length: 48  Bit Score: 36.20  E-value: 2.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034654511 241 DISLLPERAiLQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAI 285
Cdd:cd22134     4 DIQLPRELA-LKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
 240-282 3.61e-03

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. 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: 438949  Cd Length: 43  Bit Score: 36.03  E-value: 3.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654511 240 CDISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 282
Cdd:cd22178     1 VDWGNLLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 12-44 5.89e-03

dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), 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 may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.


Pssm-ID: 438530  Cd Length: 43  Bit Score: 35.47  E-value: 5.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1034654511  12 KNYFKENYIP---QALLCGILVTCPEDPLRYLEGMI 44
Cdd:cd22961     5 EEYLEKHKIPelfESLLTALLIEKPEDPIEFLIDKL 40
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 245-272 6.12e-03

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, is 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: 438893  Cd Length: 35  Bit Score: 35.03  E-value: 6.12e-03
                          10        20
                  ....*....|....*....|....*...
gi 1034654511 245 LPERAILQIFFYLSLKDVIICGQVNHAW 272
Cdd:cd22121     3 LPEEILVHIFRHLSLRDRYAAAQVCKHW 30
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
641-665 9.87e-03

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.30  E-value: 9.87e-03
                           10        20
                   ....*....|....*....|....*
gi 1034654511  641 KKLKELSVSECYRITDDGIQAFCKS 665
Cdd:smart00367   2 PNLRELDLSGCTNITDEGLQALAKG 26
 
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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