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Conserved domains on  [gi|560592195|ref|NP_001274079|]
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F-box and leucine-rich repeat protein 13 isoform 3 [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 ...
 439-619 4.58e-19

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


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 86.61  E-value: 4.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 439 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 516
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 517 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 587
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 560592195 588 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 619
Cdd:cd09293  169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 155-196 2.31e-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: 73.14  E-value: 2.31e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 560592195 155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 196
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 222-407 2.85e-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: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 222 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 300
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 301 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 374
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170       180       190
                 ....*....|....*....|....*....|...
gi 560592195 375 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 407
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 ...
 22-134 5.40e-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: 43.05  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195   22 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 100
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 560592195  101 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 134
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 ...
 439-619 4.58e-19

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 86.61  E-value: 4.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 439 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 516
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 517 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 587
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 560592195 588 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 619
Cdd:cd09293  169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 155-196 2.31e-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: 73.14  E-value: 2.31e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 560592195 155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 196
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 222-407 2.85e-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: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 222 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 300
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 301 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 374
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170       180       190
                 ....*....|....*....|....*....|...
gi 560592195 375 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 407
Cdd:cd09293  186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 155-199 7.50e-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: 7.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 560592195  155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 199
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
189-545 1.23e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.92  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 189 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 268
Cdd:COG4886   40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 269 gCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftdkglQYLNLGN-----------GCHKLIYLDLSGCtQI 337
Cdd:COG4886  112 -LTNLESLDLSGNQLTD-----LPEELANLTNL-------------KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 338 SVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDAS 417
Cdd:COG4886  172 TD-----LPEELGNLTNLKELD---LSNN----------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLP 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 418 FKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASV 497
Cdd:COG4886  222 EPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKL 289

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 560592195 498 MKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGTDISNE 545
Cdd:COG4886  290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTL 337
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 22-134 5.40e-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: 43.05  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195   22 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 100
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 560592195  101 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 134
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 ...
 439-619 4.58e-19

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 86.61  E-value: 4.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 439 ITDSSLRSLSPL--KQLTVLNLANCVRIgDMGLKQFLdgpASMRIRELNLSNCVRLSDASVMKLSERCPNLNYLSLRNCE 516
Cdd:cd09293   14 ITQSNISQLLRIlhSGLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 517 HLTAQGIGYIV-NIFSLVSIDLSG-------TDISNEAFCKSSLILEHLDVSYCsQLSDMIIKALAIYCI-NLTSLSIAG 587
Cdd:cd09293   90 NITDSGIVALAtNCPKLQTINLGRhrnghliTDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNN 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 560592195 588 CPKITDSAMEMLSAK--CHYLHILDISGCVLLTD 619
Cdd:cd09293  169 CRNLTDQSIPAILASnyFPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 155-196 2.31e-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: 73.14  E-value: 2.31e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 560592195 155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWN 196
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 222-407 2.85e-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: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 222 NVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDESMRHISEGCPGVLCLNLSN-TTITNRTMRLLPRHFHNLQN 300
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 301 LSLAY---CRRFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRYIANSC-TGIMHLTINDMPTLTDNCVKALVEK-- 374
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170       180       190
                 ....*....|....*....|....*....|...
gi 560592195 375 CSRITSLVFTGAPHISDctFRALSACKLRKIRF 407
Cdd:cd09293  186 FPNLSVLEFRGCPLITD--FSRIILFKLWQPRL 216
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 348-496 1.80e-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: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 348 SCTGIMHLTINDMPTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA-CKLRKI----RFEGNKRVTDASFKFID 422
Cdd:cd09293   50 NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATnCPKLQTinlgRHRNGHLITDVSLSALG 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 560592195 423 KNYPNLSHIYMADCKgITDSSLRSLSPL--KQLTVLNLANCVRIGDMGLKQFLDGPASMRIRELNLSNCVRLSDAS 496
Cdd:cd09293  130 KNCTFLQTVGFAGCD-VTDKGVWELASGcsKSLERLSLNNCRNLTDQSIPAILASNYFPNLSVLEFRGCPLITDFS 204
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 554-635 6.87e-08

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 53.87  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 554 LEHLDVsYCSQLSDMIIKALaIYCINLTSLSIAGCPKITDSAMEMLSAKCHYLHILDISGCVLLTDQILEDLQIGCKQLR 633
Cdd:cd09293   30 LEWLEL-YMCPISDPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQ 107


                 ..
gi 560592195 634 IL 635
Cdd:cd09293  108 TI 109
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 155-197 4.73e-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: 4.73e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 560592195 155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNA 197
Cdd:cd22148    2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 276-513 1.92e-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: 47.35  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 276 LNLSNTTITNRTMRLLPRHFHNLQNLS-LAYCRRFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRYIAN 347
Cdd:cd00116   28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 348 SCT-GIMHLTINDM-PTLTDNCVKALVEKCSRITSLVFTGAPHISDCTFRALSA----CKLRKIRFeGNKRVTDASFKFI 421
Cdd:cd00116  107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAlranRDLKELNL-ANNGIGDAGIRAL 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 422 D---KNYPNLSHIYMADCkGITDSSLRSLS----PLKQLTVLNLANCVrIGDMGLKQFLDG--PASMRIRELNLSNCvRL 492
Cdd:cd00116  186 AeglKANCNLEVLDLNNN-GLTDEGASALAetlaSLKSLEVLNLGDNN-LTDAGAAALASAllSPNISLLTLSLSCN-DI 262

                        250       260
                 ....*....|....*....|....
gi 560592195 493 SDASVMKLSERCPN---LNYLSLR 513
Cdd:cd00116  263 TDDGAKDLAEVLAEkesLLELDLR 286
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 155-195 2.04e-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: 2.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 560592195 155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 195
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 155-199 7.50e-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: 7.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 560592195  155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAID 199
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
189-545 1.23e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.92  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 189 TQLNSLWNAIDFSSVKNVIPDKYIVSTLQRWRLNVLRLNFRGCLLRPKTFRSVSHCRNLQELNVSDCPTFTDesmrhise 268
Cdd:COG4886   40 LSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN-------- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 269 gCPGVLCLNLSNTTITNrtmrlLPRHFHNLQNLslaycrrftdkglQYLNLGN-----------GCHKLIYLDLSGCtQI 337
Cdd:COG4886  112 -LTNLESLDLSGNQLTD-----LPEELANLTNL-------------KELDLSNnqltdlpeplgNLTNLKSLDLSNN-QL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 338 SVqgfryIANSCTGIMHLTINDmptLTDNcvkalvekcsRITSLvftgAPHISDCTfralsacKLRKIRFEGNKrVTDAS 417
Cdd:COG4886  172 TD-----LPEELGNLTNLKELD---LSNN----------QITDL----PEPLGNLT-------NLEELDLSGNQ-LTDLP 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 418 FKFidKNYPNLSHIYMADCKgITDssLRSLSPLKQLTVLNLANCvRIGDMGLKQFLDgpasmRIRELNLSNCvRLSDASV 497
Cdd:COG4886  222 EPL--ANLTNLETLDLSNNQ-LTD--LPELGNLTNLEELDLSNN-QLTDLPPLANLT-----NLKTLDLSNN-QLTDLKL 289

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 560592195 498 MKLSERCPNLNYLSLRNCEHLTAQGIGYIVNIFSLVSIDLSGTDISNE 545
Cdd:COG4886  290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTL 337
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 155-195 1.86e-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: 1.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 560592195 155 ISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 195
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, ...
 156-195 3.74e-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: 3.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 560592195 156 SLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 195
Cdd:cd22132    2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41
Sfi1 pfam08457
Sfi1 spindle body protein; This is a family of fungal spindle pole body proteins that play a ...
 22-134 5.40e-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: 43.05  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195   22 FCTWRDIARTNENVVLAEKmNRAVTCYNFRLQKSVFHHWHSYMEDQKEKLKNILLriqqiIYCHKLTI-ILTKWRNTARH 100
Cdd:pfam08457 305 LSTWVTNTRDTRTRLLRHE-EEFEEHRNRKLLRSKLLKWRDQLAEQREREIAANE-----FYAPRLLQeALDAWRERHQH 378

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 560592195  101 KSK------KKEDELILKHelQLKKWknrlilkRAAAEES 134
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 ...
 156-185 2.17e-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: 2.17e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 560592195 156 SLLPERAILQIFFYLSLKDVIICGQVNHAW 185
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, ...
 154-198 2.44e-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: 2.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 560592195 154 DISLLPERAiLQIFFYLSLKDVIICGQVNHAWMLMTQLNSLWNAI 198
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 ...
 153-195 2.65e-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: 2.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 560592195 153 CDISLLPERAILQIFFYLSLKDVIICGQVNHAWMLMTQLNSLW 195
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 ...
 158-185 5.99e-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: 5.99e-03
                         10        20
                 ....*....|....*....|....*...
gi 560592195 158 LPERAILQIFFYLSLKDVIICGQVNHAW 185
Cdd:cd22121    3 LPEEILVHIFRHLSLRDRYAAAQVCKHW 30
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 549-644 8.55e-03

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 38.46  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560592195 549 KSSLILEHLdvsycSQLSDMIIKAL-AIYCINLTSLSIAGCPKItDSAMEMLSAkCHYLHILDISGCVLLTDQILEDLQI 627
Cdd:cd09293    3 PLLFILHKL-----GQITQSNISQLlRILHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQ 75

                         90
                 ....*....|....*..
gi 560592195 628 GCKQLRILKMQYCTNIS 644
Cdd:cd09293   76 SCPNLQVLDLRACENIT 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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