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Conserved domains on  [gi|755510978|ref|XP_011248071|]
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F-box and leucine-rich repeat protein 13 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 9-50 6.35e-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: 74.90  E-value: 6.35e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755510978   9 PRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22977    2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 306-475 2.47e-13

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


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 70.43  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 306 NVLRLNFRGCDFRTKTLKAVSHCKNLQELNVSDCQSFTDESMRHISEGCPGVLYLNLSN-TTITNRTMRLLPRYFHNLQN 384
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 385 LSLAY---CRKFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRNIASSC-TGIVHLTINDMPTLTDNCVKVLVEK-- 458
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170
                 ....*....|....*..
gi 755510978 459 CPRISSVVLIGSPHISD 475
Cdd:cd09293  186 FPNLSVLEFRGCPLITD 202
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 240-281 1.74e-11

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


The actual alignment was detected with superfamily member cd22124:

Pssm-ID: 459239  Cd Length: 42  Bit Score: 59.66  E-value: 1.74e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 473-605 2.05e-09

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: 58.88  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 473 ISDSAFKALSSC-DLKKIRFEGNKRISDACFKSIDRNYPGINHIYMVDCKGLTDSSLKSLSLL-KQLTVLNL---TNCIR 547
Cdd:cd09293   40 ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNcPKLQTINLgrhRNGHL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 548 IGDIGLKHF-----------FDG----PASIR---------LRELNLTNCSLLGDSSV--IRLSERCPNLHYLNLRNCEH 601
Cdd:cd09293  120 ITDVSLSALgknctflqtvgFAGcdvtDKGVWelasgcsksLERLSLNNCRNLTDQSIpaILASNYFPNLSVLEFRGCPL 199


                 ....
gi 755510978 602 LTDL 605
Cdd:cd09293  200 ITDF 203
 
Name Accession Description Interval E-value
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 9-50 6.35e-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: 74.90  E-value: 6.35e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755510978   9 PRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22977    2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 306-475 2.47e-13

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 70.43  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 306 NVLRLNFRGCDFRTKTLKAVSHCKNLQELNVSDCQSFTDESMRHISEGCPGVLYLNLSN-TTITNRTMRLLPRYFHNLQN 384
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 385 LSLAY---CRKFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRNIASSC-TGIVHLTINDMPTLTDNCVKVLVEK-- 458
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170
                 ....*....|....*..
gi 755510978 459 CPRISSVVLIGSPHISD 475
Cdd:cd09293  186 FPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 240-281 1.74e-11

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: 59.66  E-value: 1.74e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 473-605 2.05e-09

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: 58.88  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 473 ISDSAFKALSSC-DLKKIRFEGNKRISDACFKSIDRNYPGINHIYMVDCKGLTDSSLKSLSLL-KQLTVLNL---TNCIR 547
Cdd:cd09293   40 ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNcPKLQTINLgrhRNGHL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 548 IGDIGLKHF-----------FDG----PASIR---------LRELNLTNCSLLGDSSV--IRLSERCPNLHYLNLRNCEH 601
Cdd:cd09293  120 ITDVSLSALgknctflqtvgFAGcdvtDKGVWelasgcsksLERLSLNNCRNLTDQSIpaILASNYFPNLSVLEFRGCPL 199


                 ....
gi 755510978 602 LTDL 605
Cdd:cd09293  200 ITDF 203
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 240-284 1.25e-07

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 48.63  E-value: 1.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755510978  240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSID 284
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
306-422 2.33e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.62  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 306 NVLRLNFRGCDFrTKTLKAVSHCKNLQELNVSDCQsftdesMRHISE---GCPGVLYLNLSNTTITNrtmrlLPRYF--- 379
Cdd:COG4886  137 NLKELDLSNNQL-TDLPEPLGNLTNLKSLDLSNNQ------LTDLPEelgNLTNLKELDLSNNQITD-----LPEPLgnl 204

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755510978 380 HNLQNLSLAYCrKFTD--------KGLQYLNLGN----------GCHKLIYLDLSGcTQIS 422
Cdd:COG4886  205 TNLEELDLSGN-QLTDlpeplanlTNLETLDLSNnqltdlpelgNLTNLEELDLSN-NQLT 263
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 564-605 4.22e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.77  E-value: 4.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755510978  564 RLRELNLTNCSLlgdsSVIRLSERCPNLHYLNLRNCEHLTDL 605
Cdd:pfam12799   2 NLEVLDLSNNQI----TDIPPLAKLPNLETLDLSGNNKITDL 39
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
230-676 6.53e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 230 AVENRRIAFDISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSIDFSTVKNIADKCVVTTLQKWRLNVLR 309
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 310 LNfrgcDFRTKTLKAVSHCKNLQELNVSDCQSFTDesmrhisegCPGVLYLNLSNTTITNrtmrlLP---RYFHNLQNLS 386
Cdd:COG4886   81 LL----SLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPeelANLTNLKELD 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 387 LAYCrKFTD--------KGLQYLNLGN-----------GCHKLIYLDLSGcTQISvqgfrNIASSCTGIVHLTINDmptL 447
Cdd:COG4886  143 LSNN-QLTDlpeplgnlTNLKSLDLSNnqltdlpeelgNLTNLKELDLSN-NQIT-----DLPEPLGNLTNLEELD---L 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 448 TDNcvkvlvekcpRISSVvligsphisDSAFKALSScdLKKIRFEGNKrISDAcfksidrnyPGInhiymvdcKGLTdss 527
Cdd:COG4886  213 SGN----------QLTDL---------PEPLANLTN--LETLDLSNNQ-LTDL---------PEL--------GNLT--- 250

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 528 lkslsllkQLTVLNLTNCiRIGDIglkhffdgPASIRLrelnltncsllgdssvirlsercPNLHYLNLRNCeHLTDLAI 607
Cdd:COG4886  251 --------NLEELDLSNN-QLTDL--------PPLANL-----------------------TNLKTLDLSNN-QLTDLKL 289

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755510978 608 EYIASMLSLISVDLSGTLISNETSAYPSVILMASLCPSALLQHHSLHLDSQAKNFLSQDLYTRAWDVYL 676
Cdd:COG4886  290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNL 358
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
328-353 1.09e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 37.00  E-value: 1.09e-03
                           10        20
                   ....*....|....*....|....*.
gi 755510978   328 CKNLQELNVSDCQSFTDESMRHISEG 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
588-612 1.29e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 37.00  E-value: 1.29e-03
                           10        20
                   ....*....|....*....|....*
gi 755510978   588 CPNLHYLNLRNCEHLTDLAIEYIAS 612
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25
FBOX smart00256
A Receptor for Ubiquitination Targets;
243-281 3.13e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.26  E-value: 3.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 755510978   243 LPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
 
Name Accession Description Interval E-value
DD_FBXL13 cd22977
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ...
 9-50 6.35e-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: 74.90  E-value: 6.35e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755510978   9 PRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22977    2 PELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 306-475 2.47e-13

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


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 70.43  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 306 NVLRLNFRGCDFRTKTLKAVSHCKNLQELNVSDCQSFTDESMRHISEGCPGVLYLNLSN-TTITNRTMRLLPRYFHNLQN 384
Cdd:cd09293   29 GLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGIVALATNCPKLQT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 385 LSLAY---CRKFTDKGLQylNLGNGCHKLIYLDLSGCtQISVQGFRNIASSC-TGIVHLTINDMPTLTDNCVKVLVEK-- 458
Cdd:cd09293  109 INLGRhrnGHLITDVSLS--ALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAILASny 185

                        170
                 ....*....|....*..
gi 755510978 459 CPRISSVVLIGSPHISD 475
Cdd:cd09293  186 FPNLSVLEFRGCPLITD 202
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 240-281 1.74e-11

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: 59.66  E-value: 1.74e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:cd22124    1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLWS 42
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 473-605 2.05e-09

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: 58.88  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 473 ISDSAFKALSSC-DLKKIRFEGNKRISDACFKSIDRNYPGINHIYMVDCKGLTDSSLKSLSLL-KQLTVLNL---TNCIR 547
Cdd:cd09293   40 ISDPPLDQLSNCnKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNcPKLQTINLgrhRNGHL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 548 IGDIGLKHF-----------FDG----PASIR---------LRELNLTNCSLLGDSSV--IRLSERCPNLHYLNLRNCEH 601
Cdd:cd09293  120 ITDVSLSALgknctflqtvgFAGcdvtDKGVWelasgcsksLERLSLNNCRNLTDQSIpaILASNYFPNLSVLEFRGCPL 199


                 ....
gi 755510978 602 LTDL 605
Cdd:cd09293  200 ITDF 203
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 536-644 8.26e-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: 8.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 536 QLTVLNLTNCIRIgDIGLKHFFdgpASIRLRELNLTNCSLLGDSSVIRLSERCPNLHYLNLRNCEHLTDLAIEYIAS--- 612
Cdd:cd09293   29 GLEWLELYMCPIS-DPPLDQLS---NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATncp 104

                         90       100       110
                 ....*....|....*....|....*....|....
gi 755510978 613 MLSLISV--DLSGTLISnetsaYPSVILMASLCP 644
Cdd:cd09293  105 KLQTINLgrHRNGHLIT-----DVSLSALGKNCT 133
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 240-284 1.25e-07

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 48.63  E-value: 1.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755510978  240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSID 284
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 240-280 3.08e-07

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: 47.33  E-value: 3.08e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22118    1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
DD_TEX55-like cd22961
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ...
 8-50 6.01e-07

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: 46.64  E-value: 6.01e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755510978   8 TPRLRSYFRDKYIPQICEALLCGLLVTCPEDPLKYLEHMILAI 50
Cdd:cd22961    1 LEDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQI 43
DD_AK5 cd22978
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ...
 12-44 7.42e-06

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: 43.68  E-value: 7.42e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 755510978  12 RSYFRDKYIPQICEALLCGLLVTCPEDPLKYLE 44
Cdd:cd22978    5 KDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLE 37
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
306-422 2.33e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.62  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 306 NVLRLNFRGCDFrTKTLKAVSHCKNLQELNVSDCQsftdesMRHISE---GCPGVLYLNLSNTTITNrtmrlLPRYF--- 379
Cdd:COG4886  137 NLKELDLSNNQL-TDLPEPLGNLTNLKSLDLSNNQ------LTDLPEelgNLTNLKELDLSNNQITD-----LPEPLgnl 204

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755510978 380 HNLQNLSLAYCrKFTD--------KGLQYLNLGN----------GCHKLIYLDLSGcTQIS 422
Cdd:COG4886  205 TNLEELDLSGN-QLTDlpeplanlTNLETLDLSNnqltdlpelgNLTNLEELDLSN-NQLT 263
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 360-597 2.90e-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: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 360 LNLSNTTITNRTMRLLPRYFHNLQNLS-LAYCRKFT---DKGLQYL--NLGNGChKLIYLDLSGC--TQISVQGFRNIAS 431
Cdd:cd00116   28 LRLEGNTLGEEAAKALASALRPQPSLKeLCLSLNETgriPRGLQSLlqGLTKGC-GLQELDLSDNalGPDGCGVLESLLR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 432 SCT-GIVHLTINDM-PTLTDNCVKVLVEKCPRISSVVLIGSPHISDSAF---KALSS-CDLKKIRFeGNKRISDACF--- 502
Cdd:cd00116  107 SSSlQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEalaKALRAnRDLKELNL-ANNGIGDAGIral 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 503 ----------KSIDRNYPGINHIYMVD-CKGLTDSSlkslsllkQLTVLNLTNCiRIGDIGLKHFFDG--PASIRLRELN 569
Cdd:cd00116  186 aeglkancnlEVLDLNNNGLTDEGASAlAETLASLK--------SLEVLNLGDN-NLTDAGAAALASAllSPNISLLTLS 256

                        250       260       270
                 ....*....|....*....|....*....|.
gi 755510978 570 LTNCSlLGDSSVIRLSERCPN---LHYLNLR 597
Cdd:cd00116  257 LSCND-ITDDGAKDLAEVLAEkesLLELDLR 286
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 240-280 6.60e-05

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: 41.11  E-value: 6.60e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22148    2 ISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELW 42
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 238-283 1.26e-04

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: 40.44  E-value: 1.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 755510978 238 FDISvLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSI 283
Cdd:cd22134    3 FDIQ-LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 564-605 4.22e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.77  E-value: 4.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755510978  564 RLRELNLTNCSLlgdsSVIRLSERCPNLHYLNLRNCEHLTDL 605
Cdd:pfam12799   2 NLEVLDLSNNQI----TDIPPLAKLPNLETLDLSGNNKITDL 39
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
230-676 6.53e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 230 AVENRRIAFDISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSIDFSTVKNIADKCVVTTLQKWRLNVLR 309
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 310 LNfrgcDFRTKTLKAVSHCKNLQELNVSDCQSFTDesmrhisegCPGVLYLNLSNTTITNrtmrlLP---RYFHNLQNLS 386
Cdd:COG4886   81 LL----SLLLLGLTDLGDLTNLTELDLSGNEELSN---------LTNLESLDLSGNQLTD-----LPeelANLTNLKELD 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 387 LAYCrKFTD--------KGLQYLNLGN-----------GCHKLIYLDLSGcTQISvqgfrNIASSCTGIVHLTINDmptL 447
Cdd:COG4886  143 LSNN-QLTDlpeplgnlTNLKSLDLSNnqltdlpeelgNLTNLKELDLSN-NQIT-----DLPEPLGNLTNLEELD---L 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 448 TDNcvkvlvekcpRISSVvligsphisDSAFKALSScdLKKIRFEGNKrISDAcfksidrnyPGInhiymvdcKGLTdss 527
Cdd:COG4886  213 SGN----------QLTDL---------PEPLANLTN--LETLDLSNNQ-LTDL---------PEL--------GNLT--- 250

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755510978 528 lkslsllkQLTVLNLTNCiRIGDIglkhffdgPASIRLrelnltncsllgdssvirlsercPNLHYLNLRNCeHLTDLAI 607
Cdd:COG4886  251 --------NLEELDLSNN-QLTDL--------PPLANL-----------------------TNLKTLDLSNN-QLTDLKL 289

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755510978 608 EYIASMLSLISVDLSGTLISNETSAYPSVILMASLCPSALLQHHSLHLDSQAKNFLSQDLYTRAWDVYL 676
Cdd:COG4886  290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNL 358
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 240-280 7.24e-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: 38.10  E-value: 7.24e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22123    1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
 243-283 9.29e-04

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. 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: 438892  Cd Length: 44  Bit Score: 37.75  E-value: 9.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755510978 243 LPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWNSI 283
Cdd:cd22120    4 LPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
328-353 1.09e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 37.00  E-value: 1.09e-03
                           10        20
                   ....*....|....*....|....*.
gi 755510978   328 CKNLQELNVSDCQSFTDESMRHISEG 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 240-280 1.21e-03

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. 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: 438918  Cd Length: 46  Bit Score: 37.29  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22147    2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELW 42
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
588-612 1.29e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 37.00  E-value: 1.29e-03
                           10        20
                   ....*....|....*....|....*
gi 755510978   588 CPNLHYLNLRNCEHLTDLAIEYIAS 612
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 243-274 1.44e-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: 36.95  E-value: 1.44e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755510978 243 LPEQAILQIFLYLTFKDMMACSRVNRSWMAMI 274
Cdd:cd22121    3 LPEEILVHIFRHLSLRDRYAAAQVCKHWREAA 34
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 243-280 1.51e-03

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: 37.21  E-value: 1.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 755510978 243 LPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLW 41
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 240-280 1.58e-03

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796  Cd Length: 43  Bit Score: 37.13  E-value: 1.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755510978  240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLW 41
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 241-275 2.22e-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: 2.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755510978 241 SVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQ 275
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
FBOX smart00256
A Receptor for Ubiquitination Targets;
243-281 3.13e-03

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 36.26  E-value: 3.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 755510978   243 LPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLWN 281
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWF 39
F-box_ScCDC4-like cd22141
F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and ...
 240-280 7.20e-03

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. 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: 438913  Cd Length: 47  Bit Score: 35.23  E-value: 7.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 755510978 240 ISVLPEQAILQIFLYLTFKDMMACSRVNRSWMAMIQRGSLW 280
Cdd:cd22141    1 IGNLPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALW 41
 
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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