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Conserved domains on  [gi|664756748|ref|XP_008535881|]
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PREDICTED: centrosomal protein of 78 kDa isoform X3 [Equus przewalskii]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1006001)

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

CATH:  3.80.10.10
Gene Ontology:  GO:0005515
PubMed:  11751054|7583641|14747988
SCOP:  4003523

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 107-260 4.64e-07

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


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 52.87  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 107 QLCKALKCCLSASGALKNLELNGLVLRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSITLKTVNFTGC 186
Cdd:COG5238  195 EGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGN 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664756748 187 NLTWQGADHMAKILKYQTMrrheetwaeslryrrpdldcmagLRRITFNCNTlIGDLGASALAESLSEDLWLRD 260
Cdd:COG5238  275 QIGAEGAIALAKALQGNTT-----------------------LTSLDLSVNR-IGDEGAIALAEGLQGNKTLHT 324
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 107-260 4.64e-07

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: 52.87  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 107 QLCKALKCCLSASGALKNLELNGLVLRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSITLKTVNFTGC 186
Cdd:COG5238  195 EGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGN 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664756748 187 NLTWQGADHMAKILKYQTMrrheetwaeslryrrpdldcmagLRRITFNCNTlIGDLGASALAESLSEDLWLRD 260
Cdd:COG5238  275 QIGAEGAIALAKALQGNTT-----------------------LTSLDLSVNR-IGDEGAIALAEGLQGNKTLHT 324
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 100-254 1.67e-06

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: 50.43  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 100 RNKdVTFQLCKALKCCLSASGALKNLEL--NGLvlRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSIT 177
Cdd:cd00116  146 RNR-LEGASCEALAKALRANRDLKELNLanNGI--GDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKS 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664756748 178 LKTVNFTGCNLTWQGADHMAKILKyqtmrrheetwAESLRYRRPDLDCmaglrritfNCntlIGDLGASALAESLSE 254
Cdd:cd00116  223 LEVLNLGDNNLTDAGAAALASALL-----------SPNISLLTLSLSC---------ND---ITDDGAKDLAEVLAE 276
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 107-260 4.64e-07

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: 52.87  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 107 QLCKALKCCLSASGALKNLELNGLVLRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSITLKTVNFTGC 186
Cdd:COG5238  195 EGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGN 274

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 664756748 187 NLTWQGADHMAKILKYQTMrrheetwaeslryrrpdldcmagLRRITFNCNTlIGDLGASALAESLSEDLWLRD 260
Cdd:COG5238  275 QIGAEGAIALAKALQGNTT-----------------------LTSLDLSVNR-IGDEGAIALAEGLQGNKTLHT 324
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 110-255 1.48e-06

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: 51.33  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 110 KALKCCLSASGALKNLELNGLVLRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSITLKTVNFTGCNLT 189
Cdd:COG5238  282 IALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIG 361

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664756748 190 WQGADHMAKILKYQTmrrheetwaeslryrrpdldcmaGLRRITFNCNTlIGDLGASALAESLSED 255
Cdd:COG5238  362 DEGAIALAKYLEGNT-----------------------TLRELNLGKNN-IGKQGAEALIDALQTN 403
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 100-254 1.67e-06

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: 50.43  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 100 RNKdVTFQLCKALKCCLSASGALKNLEL--NGLvlRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSIT 177
Cdd:cd00116  146 RNR-LEGASCEALAKALRANRDLKELNLanNGI--GDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKS 222

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664756748 178 LKTVNFTGCNLTWQGADHMAKILKyqtmrrheetwAESLRYRRPDLDCmaglrritfNCntlIGDLGASALAESLSE 254
Cdd:cd00116  223 LEVLNLGDNNLTDAGAAALASALL-----------SPNISLLTLSLSC---------ND---ITDDGAKDLAEVLAE 276
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 109-201 5.08e-05

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: 45.81  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 109 CKALKCCLSASGALKNLELNGLVLRERDLTMLTKGLNK-SATLVNLSLANCPIGDGGLEIICQGIKNSITLKTVNFTGCN 187
Cdd:cd00116  210 ASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNK 289

                         90
                 ....*....|....
gi 664756748 188 LTWQGADHMAKILK 201
Cdd:cd00116  290 FGEEGAQLLAESLL 303
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 108-258 2.84e-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: 43.50  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 108 LCKALKCCLSAsgaLKNLELNGLVLRERDLTMLTKGLNKSATLVNLSLANCPIGDGGLEIICQGIKNSITLKTVNFTGCN 187
Cdd:cd00116  128 LAKGLKDLPPA---LEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNG 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664756748 188 LTWQGADHMAKILKYQtmrrheetwaeslryrrpdldcmAGLRRITFNCNtLIGDLGASALAESLSE------DLWL 258
Cdd:cd00116  205 LTDEGASALAETLASL-----------------------KSLEVLNLGDN-NLTDAGAAALASALLSpnisllTLSL 257
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 110-253 4.73e-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: 42.73  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664756748 110 KALKCCLSASGALKNLELngLVLRERDLTMLTKG----LNKSATLVNLSLANCPIGDGGLEIICQGIK-NSITLKTVNFT 184
Cdd:cd00116   68 RGLQSLLQGLTKGCGLQE--LDLSDNALGPDGCGvlesLLRSSSLQELKLNNNGLGDRGLRLLAKGLKdLPPALEKLVLG 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664756748 185 GCNLTWQGADHMAKILKYQTmRRHEETWA------ESLRYRRPDLDCMAGLRRITFNCNTlIGDLGASALAESLS 253
Cdd:cd00116  146 RNRLEGASCEALAKALRANR-DLKELNLAnngigdAGIRALAEGLKANCNLEVLDLNNNG-LTDEGASALAETLA 218
 
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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