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Conserved domains on  [gi|2028695531|ref|NP_001381423|]
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F-box and leucine-rich repeat protein 13 isoform 4 [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 ...
 529-737 7.72e-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: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 529 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 606
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 607 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 685
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028695531 686 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 737
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 8-50 8.05e-17

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: 74.51  E-value: 8.05e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2028695531   8 NPRLKNYFKENYIPQVCEALLCGILVTCPEDPLRYLEGMIMVI 50
Cdd:cd22977     1 DPELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 245-286 2.20e-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: 2.20e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 312-497 3.21e-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: 69.66  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 312 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 390
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 391 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 464
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2028695531 465 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 497
Cdd:cd09293   186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
Sfi1 super family cl25835
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 112-224 5.39e-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: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2028695531 191 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 224
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 ...
 529-737 7.72e-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: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 529 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 606
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 607 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 685
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028695531 686 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 737
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 8-50 8.05e-17

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: 74.51  E-value: 8.05e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2028695531   8 NPRLKNYFKENYIPQVCEALLCGILVTCPEDPLRYLEGMIMVI 50
Cdd:cd22977     1 DPELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 245-286 2.20e-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: 2.20e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 312-497 3.21e-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: 69.66  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 312 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 390
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 391 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 464
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2028695531 465 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 497
Cdd:cd09293   186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 245-289 9.20e-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: 9.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 289
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
279-638 2.06e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 279 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 358
Cdd:COG4886    40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 359 gCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftdkglQYLNLGN-----------GCHKLIYLDLSGCtQI 427
Cdd:COG4886   112 -LTNLESLDLSGNQLTD-----LPEELANLTNL-------------KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 428 SVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDAS 507
Cdd:COG4886   172 TD-----LPEELGNLTNLKELD---LSNN----------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 508 FKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASV 587
Cdd:COG4886   222 EPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKL 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2028695531 588 MKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGTDISNEGLN 638
Cdd:COG4886   290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTL 340
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 112-224 5.39e-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: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2028695531 191 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 224
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 ...
 529-737 7.72e-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: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 529 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 606
Cdd:cd09293    14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 607 HLTAQGIGYIV-NIFSLVSIDlsgtdisneglnvLSRHKKlkelsvseCYRITDDGIQAFCKSSLILEHLDVSYCsQLSD 685
Cdd:cd09293    90 NITDSGIVALAtNCPKLQTIN-------------LGRHRN--------GHLITDVSLSALGKNCTFLQTVGFAGC-DVTD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028695531 686 MIIKALAIYCI-NLTSLSIAGCPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 737
Cdd:cd09293   148 KGVWELASGCSkSLERLSLNNCRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 622-762 6.67e-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: 6.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 622 LVSIDLSGTDISNEGLNVLSRHKKLKELSVSECYRITDDGIQAFCKSSLILEHLDVSYCSQLSDMIIKALAIYCINLTSL 701
Cdd:cd09293    30 LEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTI 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2028695531 702 SI---AGCPKITDSAMEMLSAKCHYLHILDISGCvLLTDQILEDLQIGC-KQLRILKMQYCTNIS 762
Cdd:cd09293   110 NLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLT 173
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 8-50 8.05e-17

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: 74.51  E-value: 8.05e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2028695531   8 NPRLKNYFKENYIPQVCEALLCGILVTCPEDPLRYLEGMIMVI 50
Cdd:cd22977     1 DPELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 245-286 2.20e-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: 2.20e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 286
Cdd:cd22124     1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 465-711 1.71e-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: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 465 CSRITSLVFTGAPhISDCTFRALSAC-KLRKIRFEGNKRVTDASFKFIDKNYPNLSHIYMADCKGITDSSLRSLSP-LKQ 542
Cdd:cd09293    27 HSGLEWLELYMCP-ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 543 LTVLNLancvrigdmGLKQfldgpasmrirelnlsNCVRLSDASVMKLSERCPNLNylslrncehltaqgigyivnifsl 622
Cdd:cd09293   106 LQTINL---------GRHR----------------NGHLITDVSLSALGKNCTFLQ------------------------ 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 623 vSIDLSGTDISNEGLNVLSRH--KKLKELSVSECYRITDDGIqafcksSLILEHLdvsycsqlsdmiikalaiYCINLTS 700
Cdd:cd09293   137 -TVGFAGCDVTDKGVWELASGcsKSLERLSLNNCRNLTDQSI------PAILASN------------------YFPNLSV 191

                         250
                  ....*....|.
gi 2028695531 701 LSIAGCPKITD 711
Cdd:cd09293   192 LEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 312-497 3.21e-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: 69.66  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 312 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 390
Cdd:cd09293    29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 391 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 464
Cdd:cd09293   109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2028695531 465 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 497
Cdd:cd09293   186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 419-586 1.96e-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: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 419 LDLSGCtQISVQGFRYIANsCTGIMHLTINDMPTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA-CKLRKI-- 495
Cdd:cd09293    33 LELYMC-PISDPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTin 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 496 --RFEGNKRVTDASFKFIDKNYPNLSHIYMADCKgITDSSLRSLSPL--KQLTVLNLANCVRIGDMGLKQFLDGPASMRI 571
Cdd:cd09293   111 lgRHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGcsKSLERLSLNNCRNLTDQSIPAILASNYFPNL 189

                         170
                  ....*....|....*
gi 2028695531 572 RELNLSNCVRLSDAS 586
Cdd:cd09293   190 SVLEFRGCPLITDFS 204
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 245-287 5.74e-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: 5.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNA 287
Cdd:cd22148     2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 12-47 1.83e-05

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: 42.40  E-value: 1.83e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2028695531  12 KNYFKENYIPQVCEALLCGILVTCPEDPLRYLEGMI 47
Cdd:cd22961     5 EEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKL 40
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 245-285 2.39e-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: 2.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22118     1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 366-603 3.21e-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: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 366 LNLSNTTITNRTMRLLPRHFHNLQNLS-LAYCRRFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRYIAN 437
Cdd:cd00116    28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 438 SCT-GIMHLTINDM-PTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA----CKLRKIRFeGNKRVTDASFKFI 511
Cdd:cd00116   107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAlranRDLKELNL-ANNGIGDAGIRAL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 512 D---KNYPNLSHIYMADCkGITDSSLRSLS----PLKQLTVLNLANCVrIGDMGLKQFLDG--PASMRIRELNLSNCvRL 582
Cdd:cd00116   186 AeglKANCNLEVLDLNNN-GLTDEGASALAetlaSLKSLEVLNLGDNN-LTDAGAAALASAllSPNISLLTLSLSCN-DI 262

                         250       260
                  ....*....|....*....|....
gi 2028695531 583 SDASVMKLSERCPN---LNYLSLR 603
Cdd:cd00116   263 TDDGAKDLAEVLAEkesLLELDLR 286
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 12-44 6.65e-05

dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 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: 438547  Cd Length: 44  Bit Score: 40.98  E-value: 6.65e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2028695531  12 KNYFKENYIPQVCEALLCGILVTCPEDPLRYLE 44
Cdd:cd22978     5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLE 37
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 245-289 9.20e-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: 9.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 289
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
279-638 2.06e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 279 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 358
Cdd:COG4886    40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 359 gCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftdkglQYLNLGN-----------GCHKLIYLDLSGCtQI 427
Cdd:COG4886   112 -LTNLESLDLSGNQLTD-----LPEELANLTNL-------------KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 428 SVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDAS 507
Cdd:COG4886   172 TD-----LPEELGNLTNLKELD---LSNN----------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 508 FKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASV 587
Cdd:COG4886   222 EPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKL 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2028695531 588 MKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGTDISNEGLN 638
Cdd:COG4886   290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTL 340
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 245-285 2.39e-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: 2.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2028695531 245 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22123     1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 246-285 4.54e-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: 38.36  E-value: 4.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2028695531 246 SLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 112-224 5.39e-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: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028695531 112 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 190
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2028695531 191 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 224
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 ...
 246-275 2.49e-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: 2.49e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2028695531 246 SLLPERAILQIFFYLSLKDVIICGQVNHAW 275
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, ...
 244-288 3.02e-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: 3.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2028695531 244 DISLLPERAiLQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAI 288
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 ...
 243-285 3.59e-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: 3.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2028695531 243 CDISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 285
Cdd:cd22178     1 VDWGNLLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 248-275 6.20e-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: 6.20e-03
                          10        20
                  ....*....|....*....|....*...
gi 2028695531 248 LPERAILQIFFYLSLKDVIICGQVNHAW 275
Cdd:cd22121     3 LPEEILVHIFRHLSLRDRYAAAQVCKHW 30
 
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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