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Conserved domains on  [gi|393202557|ref|NP_001257309|]
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X-ray radiation resistance-associated protein 1 isoform 2 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 11469232)

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

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
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-275 2.29e-17

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 84.60  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 113 NDFKHFHSVIYINASENL---LPlEAFHTFPALKELDLAFNGIKTIYVKYGDFKLLEFLDLSFNSLTvEAICDLGILPHL 189
Cdd:COG4886  130 EELANLTNLKELDLSNNQltdLP-EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNL 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 190 RVLLLTGNGLTSLPPNLAvaeqeasvtsltskryilRFPALETLMLDDNRLSNpscFASLAGLRRLKKLSLDENRIIRIP 269
Cdd:COG4886  208 EELDLSGNQLTDLPEPLA------------------NLTNLETLDLSNNQLTD---LPELGNLTNLEELDLSNNQLTDLP 266


                 ....*.
gi 393202557 270 YLQQVQ 275
Cdd:COG4886  267 PLANLT 272
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-275 2.29e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 84.60  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 113 NDFKHFHSVIYINASENL---LPlEAFHTFPALKELDLAFNGIKTIYVKYGDFKLLEFLDLSFNSLTvEAICDLGILPHL 189
Cdd:COG4886  130 EELANLTNLKELDLSNNQltdLP-EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNL 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 190 RVLLLTGNGLTSLPPNLAvaeqeasvtsltskryilRFPALETLMLDDNRLSNpscFASLAGLRRLKKLSLDENRIIRIP 269
Cdd:COG4886  208 EELDLSGNQLTDLPEPLA------------------NLTNLETLDLSNNQLTD---LPELGNLTNLEELDLSNNQLTDLP 266


                 ....*.
gi 393202557 270 YLQQVQ 275
Cdd:COG4886  267 PLANLT 272
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 124-270 4.39e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.76  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 124 INASENLL----PLEAFHTFPALKELDLAFNGIkTIYVKYGDFKLLEFLDLSFNSLTVEAICDLGILPHLRVLLLTGNGL 199
Cdd:PLN00113  98 INLSNNQLsgpiPDDIFTTSSSLRYLNLSNNNF-TGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVL 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 393202557 200 TSLPPNlavaeqeaSVTSLTSkryilrfpaLETLMLDDNRLSNpSCFASLAGLRRLKKLSLDENRII-RIPY 270
Cdd:PLN00113 177 VGKIPN--------SLTNLTS---------LEFLTLASNQLVG-QIPRELGQMKSLKWIYLGYNNLSgEIPY 230
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 170-268 1.25e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 170 LSFNSLTVEAICDLGILPHLRVLLLTGNGLTSLPpNLAvaeqeasvtsltskryilRFPALETLMLDDNRLSnpsCFASL 249
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIE-NLE------------------FLTNLTHLYLQNNQIE---KIENL 64

                         90
                 ....*....|....*....
gi 393202557 250 AGLRRLKKLSLDENRIIRI 268
Cdd:cd21340   65 ENLVNLKKLYLGGNRISVV 83
LRR_8 pfam13855
Leucine rich repeat;
187-265 1.66e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.82  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557  187 PHLRVLLLTGNGLTSLPPnlavaeqeasvtsltskRYILRFPALETLMLDDNRLS--NPSCFaslAGLRRLKKLSLDENR 264
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDD-----------------GAFKGLSNLKVLDLSNNLLTtlSPGAF---SGLPSLRYLDLSGNR 60


                  .
gi 393202557  265 I 265
Cdd:pfam13855  61 L 61
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-275 2.29e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 84.60  E-value: 2.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 113 NDFKHFHSVIYINASENL---LPlEAFHTFPALKELDLAFNGIKTIYVKYGDFKLLEFLDLSFNSLTvEAICDLGILPHL 189
Cdd:COG4886  130 EELANLTNLKELDLSNNQltdLP-EPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNL 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 190 RVLLLTGNGLTSLPPNLAvaeqeasvtsltskryilRFPALETLMLDDNRLSNpscFASLAGLRRLKKLSLDENRIIRIP 269
Cdd:COG4886  208 EELDLSGNQLTDLPEPLA------------------NLTNLETLDLSNNQLTD---LPELGNLTNLEELDLSNNQLTDLP 266


                 ....*.
gi 393202557 270 YLQQVQ 275
Cdd:COG4886  267 PLANLT 272
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-273 1.83e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 81.90  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 113 NDFKHFHSVIYINASENL---LPlEAFHTFPALKELDLAFNGIKTIYVKYGDFKLLEFLDLSFNSLTV--EAICDlgiLP 187
Cdd:COG4886  107 EELSNLTNLESLDLSGNQltdLP-EELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDlpEELGN---LT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 188 HLRVLLLTGNGLTSLPPNLAvaeqeasvtsltskryilRFPALETLMLDDNRLSNPScfASLAGLRRLKKLSLDENRIIR 267
Cdd:COG4886  183 NLKELDLSNNQITDLPEPLG------------------NLTNLEELDLSGNQLTDLP--EPLANLTNLETLDLSNNQLTD 242


                 ....*.
gi 393202557 268 IPYLQQ 273
Cdd:COG4886  243 LPELGN 248
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 124-270 4.39e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.76  E-value: 4.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 124 INASENLL----PLEAFHTFPALKELDLAFNGIkTIYVKYGDFKLLEFLDLSFNSLTVEAICDLGILPHLRVLLLTGNGL 199
Cdd:PLN00113  98 INLSNNQLsgpiPDDIFTTSSSLRYLNLSNNNF-TGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVL 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 393202557 200 TSLPPNlavaeqeaSVTSLTSkryilrfpaLETLMLDDNRLSNpSCFASLAGLRRLKKLSLDENRII-RIPY 270
Cdd:PLN00113 177 VGKIPN--------SLTNLTS---------LEFLTLASNQLVG-QIPRELGQMKSLKWIYLGYNNLSgEIPY 230
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 170-268 1.25e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 170 LSFNSLTVEAICDLGILPHLRVLLLTGNGLTSLPpNLAvaeqeasvtsltskryilRFPALETLMLDDNRLSnpsCFASL 249
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIE-NLE------------------FLTNLTHLYLQNNQIE---KIENL 64

                         90
                 ....*....|....*....
gi 393202557 250 AGLRRLKKLSLDENRIIRI 268
Cdd:cd21340   65 ENLVNLKKLYLGGNRISVV 83
LRR_8 pfam13855
Leucine rich repeat;
187-265 1.66e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.82  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557  187 PHLRVLLLTGNGLTSLPPnlavaeqeasvtsltskRYILRFPALETLMLDDNRLS--NPSCFaslAGLRRLKKLSLDENR 264
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDD-----------------GAFKGLSNLKVLDLSNNLLTtlSPGAF---SGLPSLRYLDLSGNR 60


                  .
gi 393202557  265 I 265
Cdd:pfam13855  61 L 61
LRR_8 pfam13855
Leucine rich repeat;
140-199 4.10e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 4.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393202557  140 PALKELDLAFNGIKTIYVKY-GDFKLLEFLDLSFNSLTV---EAICDLgilPHLRVLLLTGNGL 199
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTlspGAFSGL---PSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 134-265 4.32e-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: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 134 EAFHTFPALKELDLAFN-----GIKTIYVKYGDFKLLEFLDLSFNSLTVEAICDLGI----LPHLRVLLLTGNGLTSLPp 204
Cdd:cd00116  159 KALRANRDLKELNLANNgigdaGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAEtlasLKSLEVLNLGDNNLTDAG- 237

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393202557 205 nlAVAEQEASVTSLTSkryilrfpaLETLMLDDNRLSNPSCFASLAGLR---RLKKLSLDENRI 265
Cdd:cd00116  238 --AAALASALLSPNIS---------LLTLSLSCNDITDDGAKDLAEVLAekeSLLELDLRGNKF 290
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 133-269 9.65e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 40.92  E-value: 9.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 133 LEAFHTFPALKELDLAFNGIKTI----YVKYgdfklLEFLDLSF------NSLTVEAICDLGILPHLRVLLLTGNGLTSL 202
Cdd:cd21340   61 IENLENLVNLKKLYLGGNRISVVegleNLTN-----LEELHIENqrlppgEKLTFDPRSLAALSNSLRVLNISGNNIDSL 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393202557 203 PPnLAVaeqeasvtsltskryilrFPALETLMLDDNRLSNPSCFA-SLAGLRRLKKLSLDENRIIRIP 269
Cdd:cd21340  136 EP-LAP------------------LRNLEQLDASNNQISDLEELLdLLSSWPSLRELDLTGNPVCKKP 184
PLN03150 PLN03150
hypothetical protein; Provisional
 142-204 2.25e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.95  E-value: 2.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393202557 142 LKELDLAFNGIK-TIYVKYGDFKLLEFLDLSFNSLTVEAICDLGILPHLRVLLLTGNGLTSLPP 204
Cdd:PLN03150 444 LQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVP 507
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 133-274 3.46e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 39.38  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 133 LEAFHTFPALKELDLAFNGIKTIyVKYGDFKLLEFLDLSFNSLTVeaICDLGILPHLRVLLLTGN------GLTS----- 201
Cdd:cd21340   17 IDNLSLCKNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEK--IENLENLVNLKKLYLGGNrisvveGLENltnle 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 202 --------LPPNLAVAEQEASVTSLTskryilrfPALETLMLDDNRLSNPSCfasLAGLRRLKKLSLDENRIIRIPYLQQ 273
Cdd:cd21340   94 elhienqrLPPGEKLTFDPRSLAALS--------NSLRVLNISGNNIDSLEP---LAPLRNLEQLDASNNQISDLEELLD 162


                 .
gi 393202557 274 V 274
Cdd:cd21340  163 L 163
LRR_8 pfam13855
Leucine rich repeat;
131-175 8.11e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.19  E-value: 8.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 393202557  131 LPLEAFHTFPALKELDLAFNGIKTIYvkYGDF---KLLEFLDLSFNSL 175
Cdd:pfam13855  16 LDDGAFKGLSNLKVLDLSNNLLTTLS--PGAFsglPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
114-207 8.34e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 38.76  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393202557 114 DFKHFHSVIYINASENLL-PLEAFHTFPALKELDLAFNGIKTIyVKYGDFKLLEFLDLSFNSLTVEAICDLGILPHLRVL 192
Cdd:COG4886  223 PLANLTNLETLDLSNNQLtDLPELGNLTNLEELDLSNNQLTDL-PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSL 301

                         90
                 ....*....|....*
gi 393202557 193 LLTGNGLTSLPPNLA 207
Cdd:COG4886  302 LLLLLLLNLLELLIL 316
 
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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