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Conserved domains on  [gi|194018550|ref|NP_938204|]
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C-Maf-inducing protein isoform C-Mip [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];
586-771 3.46e-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: 56.48  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 586 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 665
Cdd:COG4886   37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 666 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 745
Cdd:COG4886  117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                        170       180
                 ....*....|....*....|....*....
gi 194018550 746 KLSadtyeDLK---AKLPNLKEVDVRYTE 771
Cdd:COG4886  193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
586-771 3.46e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.48  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 586 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 665
Cdd:COG4886   37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 666 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 745
Cdd:COG4886  117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                        170       180
                 ....*....|....*....|....*....
gi 194018550 746 KLSadtyeDLK---AKLPNLKEVDVRYTE 771
Cdd:COG4886  193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
594-768 1.02e-04

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: 44.24  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 594 NIIDNNDTQLQII--STLESTDVgkrmyeQLCDR-QRELKELQRKGGPTRLTLPS--KSTDADLARLLSSGSfgNLENLS 668
Cdd:cd09293   13 QITQSNISQLLRIlhSGLEWLEL------YMCPIsDPPLDQLSNCNKLKKLILPGskLIDDEGLIALAQSCP--NLQVLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 669 L-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG----DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSM--KSL 737
Cdd:cd09293   85 LrACENITDsgivALATNC---PKLQTINLGRHRNGhlitDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcsKSL 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 194018550 738 CSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 768
Cdd:cd09293  162 ERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
586-771 3.46e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.48  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 586 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 665
Cdd:COG4886   37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 666 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 745
Cdd:COG4886  117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                        170       180
                 ....*....|....*....|....*....
gi 194018550 746 KLSadtyeDLK---AKLPNLKEVDVRYTE 771
Cdd:COG4886  193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
659-771 3.85e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.48  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 659 GSFGNLENLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLC 738
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDLPEPL--GNLTNLEELDLSGNQLTDLP-EPLANLTNLE 231
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194018550 739 SLNMNSTKLSadtyeDLK--AKLPNLKEVDVRYTE 771
Cdd:COG4886  232 TLDLSNNQLT-----DLPelGNLTNLEELDLSNNQ 261
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
594-768 1.02e-04

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: 44.24  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 594 NIIDNNDTQLQII--STLESTDVgkrmyeQLCDR-QRELKELQRKGGPTRLTLPS--KSTDADLARLLSSGSfgNLENLS 668
Cdd:cd09293   13 QITQSNISQLLRIlhSGLEWLEL------YMCPIsDPPLDQLSNCNKLKKLILPGskLIDDEGLIALAQSCP--NLQVLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 669 L-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG----DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSM--KSL 737
Cdd:cd09293   85 LrACENITDsgivALATNC---PKLQTINLGRHRNGhlitDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcsKSL 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 194018550 738 CSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 768
Cdd:cd09293  162 ERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
663-771 1.27e-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: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 663 NLENLSLAFTNVTSAC----AEHLIKLPS----------------------------LKQLNLWSTQFGDAGLRLLSE-- 708
Cdd:cd00116  138 ALEKLVLGRNRLEGAScealAKALRANRDlkelnlanngigdagiralaeglkancnLEVLDLNNNGLTDEGASALAEtl 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194018550 709 -HLTMLQVLNLCETPVTDAGLLALSS-----MKSLCSLNMNSTKLSADTYEDLKAKLPN---LKEVDVRYTE 771
Cdd:cd00116  218 aSLKSLEVLNLGDNNLTDAGAAALASallspNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNK 289
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
679-769 1.72e-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: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 679 AEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHLTM---LQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLSADT 751
Cdd:COG5238  201 AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQIGDEGVIAlaeaLKNNTTVETLYLSGNQIGAEG 280
                         90       100
                 ....*....|....*....|.
gi 194018550 752 YEDLKAKL---PNLKEVDVRY 769
Cdd:COG5238  281 AIALAKALqgnTTLTSLDLSV 301
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
676-766 5.78e-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: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 676 SACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLS 748
Cdd:COG5238  254 IALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgnTTLTSLDLSVNRIGDEGAIAlaegLQGNKTLHTLNLAYNGIG 333
                         90       100
                 ....*....|....*....|.
gi 194018550 749 ADTYEDLKAKL---PNLKEVD 766
Cdd:COG5238  334 AQGAIALAKALqenTTLHSLD 354
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
652-769 6.30e-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: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194018550 652 LARLLSSGSfgNLENLSLAFTNVTS----ACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVT 724
Cdd:COG5238  256 LAEALKNNT--TVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIG 333
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194018550 725 DAG----LLALSSMKSLCSLNMNSTKLSADTYEDLkAKL----PNLKEVDVRY 769
Cdd:COG5238  334 AQGaialAKALQENTTLHSLDLSDNQIGDEGAIAL-AKYlegnTTLRELNLGK 385
 
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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