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Conserved domains on  [gi|29789255|ref|NP_085132|]
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C-Maf-inducing protein isoform Tc-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];
492-677 5.78e-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: 55.71  E-value: 5.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 492 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 571
Cdd:COG4886  37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 572 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 651
Cdd:COG4886 117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                       170       180
                ....*....|....*....|....*....
gi 29789255 652 KLSadtyeDLK---AKLPNLKEVDVRYTE 677
Cdd:COG4886 193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
492-677 5.78e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.71  E-value: 5.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 492 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 571
Cdd:COG4886  37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 572 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 651
Cdd:COG4886 117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                       170       180
                ....*....|....*....|....*....
gi 29789255 652 KLSadtyeDLK---AKLPNLKEVDVRYTE 677
Cdd:COG4886 193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
500-674 8.94e-05

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: 8.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 500 NIIDNNDTQLQII--STLESTDVgkrmyeQLCDR-QRELKELQRKGGPTRLTLPS--KSTDADLARLLSSGSfgNLENLS 574
Cdd:cd09293  13 QITQSNISQLLRIlhSGLEWLEL------YMCPIsDPPLDQLSNCNKLKKLILPGskLIDDEGLIALAQSCP--NLQVLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 575 L-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG----DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSM--KSL 643
Cdd:cd09293  85 LrACENITDsgivALATNC---PKLQTINLGRHRNGhlitDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcsKSL 161
                       170       180       190
                ....*....|....*....|....*....|....
gi 29789255 644 CSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 674
Cdd:cd09293 162 ERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
492-677 5.78e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.71  E-value: 5.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 492 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 571
Cdd:COG4886  37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 572 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 651
Cdd:COG4886 117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                       170       180
                ....*....|....*....|....*....
gi 29789255 652 KLSadtyeDLK---AKLPNLKEVDVRYTE 677
Cdd:COG4886 193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
565-677 6.64e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 6.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 565 GSFGNLENLSLAFTNVTSAcAEHLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLC 644
Cdd:COG4886 156 GNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPEPL--GNLTNLEELDLSGNQLTDLP-EPLANLTNLE 231
                        90       100       110
                ....*....|....*....|....*....|....*
gi 29789255 645 SLNMNSTKLSadtyeDLK--AKLPNLKEVDVRYTE 677
Cdd:COG4886 232 TLDLSNNQLT-----DLPelGNLTNLEELDLSNNQ 261
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
500-674 8.94e-05

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: 8.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 500 NIIDNNDTQLQII--STLESTDVgkrmyeQLCDR-QRELKELQRKGGPTRLTLPS--KSTDADLARLLSSGSfgNLENLS 574
Cdd:cd09293  13 QITQSNISQLLRIlhSGLEWLEL------YMCPIsDPPLDQLSNCNKLKKLILPGskLIDDEGLIALAQSCP--NLQVLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 575 L-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG----DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSM--KSL 643
Cdd:cd09293  85 LrACENITDsgivALATNC---PKLQTINLGRHRNGhlitDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcsKSL 161
                       170       180       190
                ....*....|....*....|....*....|....
gi 29789255 644 CSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 674
Cdd:cd09293 162 ERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
569-677 1.30e-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: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 569 NLENLSLAFTNVTSAC----AEHLIKLPS----------------------------LKQLNLWSTQFGDAGLRLLSE-- 614
Cdd:cd00116 138 ALEKLVLGRNRLEGAScealAKALRANRDlkelnlanngigdagiralaeglkancnLEVLDLNNNGLTDEGASALAEtl 217
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789255 615 -HLTMLQVLNLCETPVTDAGLLALSS-----MKSLCSLNMNSTKLSADTYEDLKAKLPN---LKEVDVRYTE 677
Cdd:cd00116 218 aSLKSLEVLNLGDNNLTDAGAAALASallspNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNK 289
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
585-675 1.63e-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: 1.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 585 AEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHLTM---LQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLSADT 657
Cdd:COG5238 201 AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQIGDEGVIAlaeaLKNNTTVETLYLSGNQIGAEG 280
                        90       100
                ....*....|....*....|.
gi 29789255 658 YEDLKAKL---PNLKEVDVRY 675
Cdd:COG5238 281 AIALAKALqgnTTLTSLDLSV 301
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
582-672 5.49e-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: 5.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 582 SACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLS 654
Cdd:COG5238 254 IALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgnTTLTSLDLSVNRIGDEGAIAlaegLQGNKTLHTLNLAYNGIG 333
                        90       100
                ....*....|....*....|.
gi 29789255 655 ADTYEDLKAKL---PNLKEVD 672
Cdd:COG5238 334 AQGAIALAKALqenTTLHSLD 354
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
558-675 5.93e-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: 5.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789255 558 LARLLSSGSfgNLENLSLAFTNVTS----ACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVT 630
Cdd:COG5238 256 LAEALKNNT--TVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIG 333
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 29789255 631 DAG----LLALSSMKSLCSLNMNSTKLSADTYEDLkAKL----PNLKEVDVRY 675
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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