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Conserved domains on  [gi|767990612|ref|XP_011521654|]
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C-Maf-inducing protein isoform X2 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1001123)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Oryctolagus cuniculus monocyte differentiation antigen CD14, a coreceptor for bacterial lipopolysaccharide

Gene Ontology:  GO:0005515
PubMed:  11751054

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
629-755 2.16e-08

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


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 629 LKELDADLARLLssgsfgNLENLSLAFTNVTSAcAEHLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVT 708
Cdd:COG4886  148 LTDLPEPLGNLT------NLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL--GNLTNLEELDLSGNQLT 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767990612 709 DAGlLALSSMKSLCSLNMNSTKLSadtyeDLK--AKLPNLKEVDVRYTE 755
Cdd:COG4886  219 DLP-EPLANLTNLETLDLSNNQLT-----DLPelGNLTNLEELDLSNNQ 261
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
629-755 2.16e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 629 LKELDADLARLLssgsfgNLENLSLAFTNVTSAcAEHLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVT 708
Cdd:COG4886  148 LTDLPEPLGNLT------NLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL--GNLTNLEELDLSGNQLT 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767990612 709 DAGlLALSSMKSLCSLNMNSTKLSadtyeDLK--AKLPNLKEVDVRYTE 755
Cdd:COG4886  219 DLP-EPLANLTNLETLDLSNNQLT-----DLPelGNLTNLEELDLSNNQ 261
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 647-755 1.33e-04

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: 44.65  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 647 NLENLSLAFTNVTSAC----AEHLIKLPS----------------------------LKQLNLWSTQFGDAGLRLLSE-- 692
Cdd:cd00116  138 ALEKLVLGRNRLEGAScealAKALRANRDlkelnlanngigdagiralaeglkancnLEVLDLNNNGLTDEGASALAEtl 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990612 693 -HLTMLQVLNLCETPVTDAGLLALSS-----MKSLCSLNMNSTKLSADTYEDLKAKLPN---LKEVDVRYTE 755
Cdd:cd00116  218 aSLKSLEVLNLGDNNLTDAGAAALASallspNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNK 289
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
629-755 2.16e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 629 LKELDADLARLLssgsfgNLENLSLAFTNVTSAcAEHLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVT 708
Cdd:COG4886  148 LTDLPEPLGNLT------NLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL--GNLTNLEELDLSGNQLT 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767990612 709 DAGlLALSSMKSLCSLNMNSTKLSadtyeDLK--AKLPNLKEVDVRYTE 755
Cdd:COG4886  219 DLP-EPLANLTNLETLDLSNNQLT-----DLPelGNLTNLEELDLSNNQ 261
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
559-755 3.72e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.40  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 559 KFLLSLAENKLGPCMLLALRGNQTMVEILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMY-EQLCDRQRELKELDadLA 637
Cdd:COG4886   27 LLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLgLTDLGDLTNLTELD--LS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 638 RLLSSGSFGNLENLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSS 717
Cdd:COG4886  105 GNEELSNLTNLESLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGN 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767990612 718 MKSLCSLNMNSTKLSadtyeDLK---AKLPNLKEVDVRYTE 755
Cdd:COG4886  181 LTNLKELDLSNNQIT-----DLPeplGNLTNLEELDLSGNQ 216
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 647-755 1.33e-04

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: 44.65  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 647 NLENLSLAFTNVTSAC----AEHLIKLPS----------------------------LKQLNLWSTQFGDAGLRLLSE-- 692
Cdd:cd00116  138 ALEKLVLGRNRLEGAScealAKALRANRDlkelnlanngigdagiralaeglkancnLEVLDLNNNGLTDEGASALAEtl 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767990612 693 -HLTMLQVLNLCETPVTDAGLLALSS-----MKSLCSLNMNSTKLSADTYEDLKAKLPN---LKEVDVRYTE 755
Cdd:cd00116  218 aSLKSLEVLNLGDNNLTDAGAAALASallspNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNK 289
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 663-753 1.68e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.78  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 663 AEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHLTM---LQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLSADT 735
Cdd:COG5238  201 AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQIGDEGVIAlaeaLKNNTTVETLYLSGNQIGAEG 280

                         90       100
                 ....*....|....*....|.
gi 767990612 736 YEDLKAKL---PNLKEVDVRY 753
Cdd:COG5238  281 AIALAKALqgnTTLTSLDLSV 301
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 660-750 5.73e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 43.24  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 660 SACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLS 732
Cdd:COG5238  254 IALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgnTTLTSLDLSVNRIGDEGAIAlaegLQGNKTLHTLNLAYNGIG 333

                         90       100
                 ....*....|....*....|.
gi 767990612 733 ADTYEDLKAKL---PNLKEVD 750
Cdd:COG5238  334 AQGAIALAKALqenTTLHSLD 354
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 636-753 6.14e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 42.85  E-value: 6.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 636 LARLLSSGSfgNLENLSLAFTNVTS----ACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVT 708
Cdd:COG5238  256 LAEALKNNT--TVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIG 333

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767990612 709 DAG----LLALSSMKSLCSLNMNSTKLSADTYEDLkAKL----PNLKEVDVRY 753
Cdd:COG5238  334 AQGaialAKALQENTTLHSLDLSDNQIGDEGAIAL-AKYlegnTTLRELNLGK 385
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
628-757 1.71e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 628 ELKELDADLARLlssgsfGNLENLSLAFTNVTSAcaEHLIKLPSLKQLNLWSTQFGDAGLrllSEHLTMLQVLNLCETPV 707
Cdd:COG4886  216 QLTDLPEPLANL------TNLETLDLSNNQLTDL--PELGNLTNLEELDLSNNQLTDLPP---LANLTNLKTLDLSNNQL 284

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767990612 708 TDAGLLALSSMKSLCSLNMNSTKLSADTYEDLKAKLPNLKEVDVRYTEAW 757
Cdd:COG4886  285 TDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLL 334
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 647-752 3.75e-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: 39.62  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 647 NLENLSL-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG----DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSS 717
Cdd:cd09293   79 NLQVLDLrACENITDsgivALATNC---PKLQTINLGRHRNGhlitDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELAS 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767990612 718 M--KSLCSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 752
Cdd:cd09293  156 GcsKSLERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 633-716 4.33e-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: 39.23  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990612 633 DADLARLLSSgSFGNLENLSLAFTNVTSACAEHLIKLPSLKQLNL-WSTQFGDAGLRLLSEHLTMLQVLNL--CETpVTD 709
Cdd:cd09293   16 QSNISQLLRI-LHSGLEWLELYMCPISDPPLDQLSNCNKLKKLILpGSKLIDDEGLIALAQSCPNLQVLDLraCEN-ITD 93


                 ....*..
gi 767990612 710 AGLLALS 716
Cdd:cd09293   94 SGIVALA 100
 
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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