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Conserved domains on  [gi|15222749|ref|NP_175955|]
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RNI-like superfamily protein [Arabidopsis thaliana]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1563018)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 351-511 4.93e-16

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: 77.37  E-value: 4.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 351 SDLAFHDVTgSSCSLQEVRLSTCPLITSEAVKKLGL-CGNLEVLDLGSCKSISDSCLNSVSA-LRKLTSLNLA----GAD 424
Cdd:cd09293  41 SDPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQsCPNLQVLDLRACENITDSGIVALATnCPKLQTINLGrhrnGHL 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 425 VTDSGMLALGKSDVPITQLSLRGCRrVSDRGISYLLNNEGtisKTLSTLDLGHMPGISDRAIHTI--THCCKALTELSIR 502
Cdd:cd09293 120 ITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCS---KSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFR 195


                ....*....
gi 15222749 503 SCFHVTDSS 511
Cdd:cd09293 196 GCPLITDFS 204
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 351-511 4.93e-16

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: 77.37  E-value: 4.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 351 SDLAFHDVTgSSCSLQEVRLSTCPLITSEAVKKLGL-CGNLEVLDLGSCKSISDSCLNSVSA-LRKLTSLNLA----GAD 424
Cdd:cd09293  41 SDPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQsCPNLQVLDLRACENITDSGIVALATnCPKLQTINLGrhrnGHL 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 425 VTDSGMLALGKSDVPITQLSLRGCRrVSDRGISYLLNNEGtisKTLSTLDLGHMPGISDRAIHTI--THCCKALTELSIR 502
Cdd:cd09293 120 ITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCS---KSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFR 195


                ....*....
gi 15222749 503 SCFHVTDSS 511
Cdd:cd09293 196 GCPLITDFS 204
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 267-486 1.58e-03

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: 41.31  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 267 YTGLQAL-GFCQQLTSLSLVRTcynrkISFKR--INDMGIFLLSEACKGLESVR---LGGfPKVSDAGFASLLHSCRN-- 338
Cdd:COG5238 191 QIGDEGIeELAEALTQNTTVTT-----LWLKRnpIGDEGAEILAEALKGNKSLTtldLSN-NQIGDEGVIALAEALKNnt 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 339 --------LKKFEVRGAFLLSDLafhdVTGSScSLQEVRLSTCPlITSEAVKKL--GLCGN--LEVLDLGSCKsISDSCL 406
Cdd:COG5238 265 tvetlylsGNQIGAEGAIALAKA----LQGNT-TLTSLDLSVNR-IGDEGAIALaeGLQGNktLHTLNLAYNG-IGAQGA 337

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 407 NSVSA----LRKLTSLNLAGADVTDSGMLALGKSDVPITQ---LSLRGcRRVSDRGISYLLNNEGTISKTLSTLDLGHMP 479
Cdd:COG5238 338 IALAKalqeNTTLHSLDLSDNQIGDEGAIALAKYLEGNTTlreLNLGK-NNIGKQGAEALIDALQTNRLHTLILDGNLIG 416


                ....*..
gi 15222749 480 GISDRAI 486
Cdd:COG5238 417 AEAQQRL 423
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
493-516 5.96e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.69  E-value: 5.96e-03
                           10        20
                   ....*....|....*....|....
gi 15222749    493 CKALTELSIRSCFHVTDSSIESLA 516
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 351-511 4.93e-16

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: 77.37  E-value: 4.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 351 SDLAFHDVTgSSCSLQEVRLSTCPLITSEAVKKLGL-CGNLEVLDLGSCKSISDSCLNSVSA-LRKLTSLNLA----GAD 424
Cdd:cd09293  41 SDPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQsCPNLQVLDLRACENITDSGIVALATnCPKLQTINLGrhrnGHL 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 425 VTDSGMLALGKSDVPITQLSLRGCRrVSDRGISYLLNNEGtisKTLSTLDLGHMPGISDRAIHTI--THCCKALTELSIR 502
Cdd:cd09293 120 ITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCS---KSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFR 195


                ....*....
gi 15222749 503 SCFHVTDSS 511
Cdd:cd09293 196 GCPLITDFS 204
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 218-484 1.40e-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: 58.49  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 218 SFTLQSLSLVLDLISDRLIIAItgsLPQLVKLDLEDRPEKEPFPDNdltytglqaLGFCQQLTSLSLvrtcynrkISFKR 297
Cdd:cd09293   5 LFILHKLGQITQSNISQLLRIL---HSGLEWLELYMCPISDPPLDQ---------LSNCNKLKKLIL--------PGSKL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 298 INDMGIFLLSEACKGLESVRLGGFPKVSDAGFASLLHSCRNLKKFEVRgafllsdlafhdvtgsscslqevRLSTCPLIT 377
Cdd:cd09293  65 IDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLG-----------------------RHRNGHLIT 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 378 SEAVKKLGlcgnlevldlGSCksisdsclnsvsalRKLTSLNLAGADVTDSGM--LALGKSDvPITQLSLRGCRRVSDRG 455
Cdd:cd09293 122 DVSLSALG----------KNC--------------TFLQTVGFAGCDVTDKGVweLASGCSK-SLERLSLNNCRNLTDQS 176

                       250       260
                ....*....|....*....|....*....
gi 15222749 456 ISYLLNNEGTisKTLSTLDLGHMPGISDR 484
Cdd:cd09293 177 IPAILASNYF--PNLSVLEFRGCPLITDF 203
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 267-486 1.58e-03

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: 41.31  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 267 YTGLQAL-GFCQQLTSLSLVRTcynrkISFKR--INDMGIFLLSEACKGLESVR---LGGfPKVSDAGFASLLHSCRN-- 338
Cdd:COG5238 191 QIGDEGIeELAEALTQNTTVTT-----LWLKRnpIGDEGAEILAEALKGNKSLTtldLSN-NQIGDEGVIALAEALKNnt 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 339 --------LKKFEVRGAFLLSDLafhdVTGSScSLQEVRLSTCPlITSEAVKKL--GLCGN--LEVLDLGSCKsISDSCL 406
Cdd:COG5238 265 tvetlylsGNQIGAEGAIALAKA----LQGNT-TLTSLDLSVNR-IGDEGAIALaeGLQGNktLHTLNLAYNG-IGAQGA 337

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 407 NSVSA----LRKLTSLNLAGADVTDSGMLALGKSDVPITQ---LSLRGcRRVSDRGISYLLNNEGTISKTLSTLDLGHMP 479
Cdd:COG5238 338 IALAKalqeNTTLHSLDLSDNQIGDEGAIALAKYLEGNTTlreLNLGK-NNIGKQGAEALIDALQTNRLHTLILDGNLIG 416


                ....*..
gi 15222749 480 GISDRAI 486
Cdd:COG5238 417 AEAQQRL 423
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
493-516 5.96e-03

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


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 34.69  E-value: 5.96e-03
                           10        20
                   ....*....|....*....|....
gi 15222749    493 CKALTELSIRSCFHVTDSSIESLA 516
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 361-534 8.41e-03

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: 38.49  E-value: 8.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 361 SSCSLQEVRLSTCPL-ITSEAVKKLGLCG---NLEVLDLGSCKSISDSC---LNSVSALRKLTSLNLAGADVTDSGMLAL 433
Cdd:cd00116 106 RSSSLQELKLNNNGLgDRGLRLLAKGLKDlppALEKLVLGRNRLEGASCealAKALRANRDLKELNLANNGIGDAGIRAL 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222749 434 ---GKSDVPITQLSLRGCrRVSDRGISYLlnnEGTIS--KTLSTLDLGHMPgISDRAIHTIthcCKALTELSIR------ 502
Cdd:cd00116 186 aegLKANCNLEVLDLNNN-GLTDEGASAL---AETLAslKSLEVLNLGDNN-LTDAGAAAL---ASALLSPNISlltlsl 257

                       170       180       190
                ....*....|....*....|....*....|..
gi 15222749 503 SCFHVTDSSIESLAtwERQAEggSKQLRKLNV 534
Cdd:cd00116 258 SCNDITDDGAKDLA--EVLAE--KESLLELDL 285
 
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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