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Conserved domains on  [gi|1034596156|ref|XP_016879222|]
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C-Maf-inducing protein isoform X5 [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];
399-584 6.38e-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: 55.32  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 399 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 478
Cdd:COG4886    37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 479 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 558
Cdd:COG4886   117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                         170       180
                  ....*....|....*....|....*....
gi 1034596156 559 KLSadtyeDLK---AKLPNLKEVDVRYTE 584
Cdd:COG4886   193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
399-584 6.38e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 399 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 478
Cdd:COG4886    37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 479 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 558
Cdd:COG4886   117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                         170       180
                  ....*....|....*....|....*....
gi 1034596156 559 KLSadtyeDLK---AKLPNLKEVDVRYTE 584
Cdd:COG4886   193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
442-581 1.47e-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: 43.47  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 442 LKELQRKGGPTRLTLPS--KSTDADLARLLSSGSfgNLENLSL-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG-- 512
Cdd:cd09293    45 LDQLSNCNKLKKLILPGskLIDDEGLIALAQSCP--NLQVLDLrACENITDsgivALATNC---PKLQTINLGRHRNGhl 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596156 513 --DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSM--KSLCSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 581
Cdd:cd09293   120 itDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcsKSLERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
399-584 6.38e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 399 ILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLE 478
Cdd:COG4886    37 LLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 479 NLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLCSLNMNST 558
Cdd:COG4886   117 SLDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL--GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNN 192
                         170       180
                  ....*....|....*....|....*....
gi 1034596156 559 KLSadtyeDLK---AKLPNLKEVDVRYTE 584
Cdd:COG4886   193 QIT-----DLPeplGNLTNLEELDLSGNQ 216
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
472-584 6.73e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.94  E-value: 6.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 472 GSFGNLENLSLAFTNVTSACAEhLIKLPSLKQLNLWSTQFGDAGLRLlsEHLTMLQVLNLCETPVTDAGlLALSSMKSLC 551
Cdd:COG4886   156 GNLTNLKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDLPEPL--GNLTNLEELDLSGNQLTDLP-EPLANLTNLE 231
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034596156 552 SLNMNSTKLSadtyeDLK--AKLPNLKEVDVRYTE 584
Cdd:COG4886   232 TLDLSNNQLT-----DLPelGNLTNLEELDLSNNQ 261
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
492-582 1.45e-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: 44.40  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 492 AEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHLTM---LQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLSADT 564
Cdd:COG5238   201 AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGnksLTTLDLSNNQIGDEGVIAlaeaLKNNTTVETLYLSGNQIGAEG 280
                          90       100
                  ....*....|....*....|.
gi 1034596156 565 YEDLKAKL---PNLKEVDVRY 582
Cdd:COG5238   281 AIALAKALqgnTTLTSLDLSV 301
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
442-581 1.47e-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: 43.47  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 442 LKELQRKGGPTRLTLPS--KSTDADLARLLSSGSfgNLENLSL-AFTNVTS----ACAEHLiklPSLKQLNLWSTQFG-- 512
Cdd:cd09293    45 LDQLSNCNKLKKLILPGskLIDDEGLIALAQSCP--NLQVLDLrACENITDsgivALATNC---PKLQTINLGRHRNGhl 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034596156 513 --DAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSM--KSLCSLNMNS-TKLSADTYEDLKAKL--PNLKEVDVR 581
Cdd:cd09293   120 itDVSLSALGKNCTFLQTVGFAGCDVTDKGVWELASGcsKSLERLSLNNcRNLTDQSIPAILASNyfPNLSVLEFR 195
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
476-584 2.02e-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: 43.88  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 476 NLENLSLAFTNVTSAC----AEHLIKLPS----------------------------LKQLNLWSTQFGDAGLRLLSE-- 521
Cdd:cd00116   138 ALEKLVLGRNRLEGAScealAKALRANRDlkelnlanngigdagiralaeglkancnLEVLDLNNNGLTDEGASALAEtl 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034596156 522 -HLTMLQVLNLCETPVTDAGLLALSS-----MKSLCSLNMNSTKLSADTYEDLKAKLPN---LKEVDVRYTE 584
Cdd:cd00116   218 aSLKSLEVLNLGDNNLTDAGAAALASallspNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNK 289
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
489-579 4.84e-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: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 489 SACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVTDAGLLA----LSSMKSLCSLNMNSTKLS 561
Cdd:COG5238   254 IALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgnTTLTSLDLSVNRIGDEGAIAlaegLQGNKTLHTLNLAYNGIG 333
                          90       100
                  ....*....|....*....|.
gi 1034596156 562 ADTYEDLKAKL---PNLKEVD 579
Cdd:COG5238   334 AQGAIALAKALqenTTLHSLD 354
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
465-582 5.19e-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: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596156 465 LARLLSSGSfgNLENLSLAFTNVTS----ACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHL---TMLQVLNLCETPVT 537
Cdd:COG5238   256 LAEALKNNT--TVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIG 333
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034596156 538 DAG----LLALSSMKSLCSLNMNSTKLSADTYEDLkAKL----PNLKEVDVRY 582
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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