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Conserved domains on  [gi|186511493|ref|NP_001118925|]
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Outer arm dynein light chain 1 protein [Arabidopsis thaliana]

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];
413-597 6.27e-23

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.93  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 413 PFLSAFVGLRVLNLSGNAIVRITA--GALPRgLHALNLSKNSISVI-EGLRELTRLRVLDLSYNRILRLGHGLASCSSLK 489
Cdd:COG4886  153 EPLGNLTNLKSLDLSNNQLTDLPEelGNLTN-LKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 490 ELYLAGNKISEIEGLHRLLKLTVLDLRFNKFSTTKCLGQLaanySSLQAISLEGNPAQKNVGDEQLRKYLLGLLPNLVYY 569
Cdd:COG4886  232 TLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANL----TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307

                        170       180
                 ....*....|....*....|....*...
gi 186511493 570 NRQGTKDARLGTSTHQLDRGLRSELKNS 597
Cdd:COG4886  308 LNLLELLILLLLLTTLLLLLLLLKGLLV 335
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
413-597 6.27e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.93  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 413 PFLSAFVGLRVLNLSGNAIVRITA--GALPRgLHALNLSKNSISVI-EGLRELTRLRVLDLSYNRILRLGHGLASCSSLK 489
Cdd:COG4886  153 EPLGNLTNLKSLDLSNNQLTDLPEelGNLTN-LKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 490 ELYLAGNKISEIEGLHRLLKLTVLDLRFNKFSTTKCLGQLaanySSLQAISLEGNPAQKNVGDEQLRKYLLGLLPNLVYY 569
Cdd:COG4886  232 TLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANL----TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307

                        170       180
                 ....*....|....*....|....*...
gi 186511493 570 NRQGTKDARLGTSTHQLDRGLRSELKNS 597
Cdd:COG4886  308 LNLLELLILLLLLTTLLLLLLLLKGLLV 335
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 404-549 2.41e-20

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: 90.23  E-value: 2.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 404 LVSHGLVVIPFLSAFVGLRVLNLSGNAIVRITA-GALPRgLHALNLSKNSISVIEGLRELTRLRVLDLSYNRILRLGhGL 482
Cdd:cd21340    9 LNDKNITKIDNLSLCKNLKVLYLYDNKITKIENlEFLTN-LTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVE-GL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 483 ASCSSLKELYL------------------------------AGNKISEIEGLHRLLKLTVLDLRFNKFSTTKCLGQLAAN 532
Cdd:cd21340   87 ENLTNLEELHIenqrlppgekltfdprslaalsnslrvlniSGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDLLSS 166

                        170
                 ....*....|....*..
gi 186511493 533 YSSLQAISLEGNPAQKN 549
Cdd:cd21340  167 WPSLRELDLTGNPVCKK 183
LRR_8 pfam13855
Leucine rich repeat;
463-520 1.14e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.06  E-value: 1.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511493  463 TRLRVLDLSYNRILRLGHG-LASCSSLKELYLAGNKISEIEG--LHRLLKLTVLDLRFNKF 520
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 415-475 1.19e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511493 415 LSAFVGLRVLNLSGNAI---VRITAGALPrGLHALNLSKNSI--SVIEGLRELTRLRVLDLSYNRI 475
Cdd:PLN03150 438 ISKLRHLQSINLSGNSIrgnIPPSLGSIT-SLEVLDLSYNSFngSIPESLGQLTSLRILNLNGNSL 502
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
413-597 6.27e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.93  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 413 PFLSAFVGLRVLNLSGNAIVRITA--GALPRgLHALNLSKNSISVI-EGLRELTRLRVLDLSYNRILRLGHGLASCSSLK 489
Cdd:COG4886  153 EPLGNLTNLKSLDLSNNQLTDLPEelGNLTN-LKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 490 ELYLAGNKISEIEGLHRLLKLTVLDLRFNKFSTTKCLGQLaanySSLQAISLEGNPAQKNVGDEQLRKYLLGLLPNLVYY 569
Cdd:COG4886  232 TLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANL----TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307

                        170       180
                 ....*....|....*....|....*...
gi 186511493 570 NRQGTKDARLGTSTHQLDRGLRSELKNS 597
Cdd:COG4886  308 LNLLELLILLLLLTTLLLLLLLLKGLLV 335
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
404-544 2.89e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.01  E-value: 2.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 404 LVSHGLVVIP-FLSAFVGLRVLNLSGNAIVRITA--GALPRgLHALNLSKNSISVI-EGLRELTRLRVLDLSYNRILRLG 479
Cdd:COG4886  120 LSGNQLTDLPeELANLTNLKELDLSNNQLTDLPEplGNLTN-LKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLP 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511493 480 HGLASCSSLKELYLAGNKISEI-EGLHRLLKLTVLDLRFNKFSTTKCLGQLaanySSLQAISLEGN 544
Cdd:COG4886  199 EPLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNL----TNLEELDLSNN 260
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 404-549 2.41e-20

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: 90.23  E-value: 2.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 404 LVSHGLVVIPFLSAFVGLRVLNLSGNAIVRITA-GALPRgLHALNLSKNSISVIEGLRELTRLRVLDLSYNRILRLGhGL 482
Cdd:cd21340    9 LNDKNITKIDNLSLCKNLKVLYLYDNKITKIENlEFLTN-LTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVE-GL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 483 ASCSSLKELYL------------------------------AGNKISEIEGLHRLLKLTVLDLRFNKFSTTKCLGQLAAN 532
Cdd:cd21340   87 ENLTNLEELHIenqrlppgekltfdprslaalsnslrvlniSGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDLLSS 166

                        170
                 ....*....|....*..
gi 186511493 533 YSSLQAISLEGNPAQKN 549
Cdd:cd21340  167 WPSLRELDLTGNPVCKK 183
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
415-544 3.13e-18

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 87.68  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 415 LSAFVGLRVLNLSGNAIVRITA--GALPRgLHALNLSKNSISVI-EGLRELTRLRVLDLSYNRILRLGHGLASCSSLKEL 491
Cdd:COG4886  109 LSNLTNLESLDLSGNQLTDLPEelANLTN-LKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKEL 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186511493 492 YLAGNKISEI-EGLHRLLKLTVLDLRFNKFST-TKCLGQLaanySSLQAISLEGN 544
Cdd:COG4886  188 DLSNNQITDLpEPLGNLTNLEELDLSGNQLTDlPEPLANL----TNLETLDLSNN 238
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 424-515 1.64e-14

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: 73.28  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 424 LNLSGNAIVRITAGALPRGLHALNLSKNSISVIEGLRELTRLRVLDLSYNRILRLGhGLASCSSLKELYLAGNKISEIEG 503
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISVVEG 85

                         90
                 ....*....|..
gi 186511493 504 LHRLLKLTVLDL 515
Cdd:cd21340   86 LENLTNLEELHI 97
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
415-545 2.00e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.58  E-value: 2.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 415 LSAFVGLRVLNLSGNAIVRITAGALPRGLHALNLSKNsisviEGLRELTRLRVLDLSYNRILRLGHGLASCSSLKELYLA 494
Cdd:COG4886   70 SLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLS 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 186511493 495 GNKISEI-EGLHRLLKLTVLDLRFNKFSTtkcLGQLAANYSSLQAISLEGNP 545
Cdd:COG4886  145 NNQLTDLpEPLGNLTNLKSLDLSNNQLTD---LPEELGNLTNLKELDLSNNQ 193
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 443-521 2.54e-11

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: 63.65  E-value: 2.54e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186511493 443 LHALNLSKNSISVIEGLRELTRLRVLDLSYNRILRLGhGLASCSSLKELYLAGNKISEIEGLHRLLKLTVLDLRFNKFS 521
Cdd:cd21340    4 ITHLYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRIS 81
LRR_8 pfam13855
Leucine rich repeat;
463-520 1.14e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.06  E-value: 1.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511493  463 TRLRVLDLSYNRILRLGHG-LASCSSLKELYLAGNKISEIEG--LHRLLKLTVLDLRFNKF 520
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
441-498 1.30e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 1.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511493  441 RGLHALNLSKNSISVIEG--LRELTRLRVLDLSYNRILRL-GHGLASCSSLKELYLAGNKI 498
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_9 pfam14580
Leucine-rich repeat;
422-524 2.94e-07

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 50.92  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493  422 RVLNLSGNAIVRIT-AGALPRGLHALNLSKNSISVIEGLRELTRLRVLDLSYNRILRLGHGLASC-SSLKELYLAGNKIS 499
Cdd:pfam14580  22 RELDLRGYKIPIIEnLGATLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEAlPNLTELILTNNNLQ 101

                          90       100
                  ....*....|....*....|....*...
gi 186511493  500 E---IEGLHRLLKLTVLDLRFNKFSTTK 524
Cdd:pfam14580 102 ElgdLDPLASLKKLTFLSLLRNPVTNKP 129
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 362-563 3.64e-07

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: 52.36  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 362 EPVVLNEQatsSAKVDAIKLTPGMEAAKKYISSLSASATTAQLVSHGL-VVIPFLSAFVGLRVLNLSGNAIVRITAGALP 440
Cdd:cd00116   26 QVLRLEGN---TLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLqSLLQGLTKGCGLQELDLSDNALGPDGCGVLE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 441 R-----GLHALNLSKNSIS------VIEGLRELT-RLRVLDLSYNRI-----LRLGHGLASCSSLKELYLAGNKISEiEG 503
Cdd:cd00116  103 SllrssSLQELKLNNNGLGdrglrlLAKGLKDLPpALEKLVLGRNRLegascEALAKALRANRDLKELNLANNGIGD-AG 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186511493 504 LHRLLK-------LTVLDLRFNKFSTTKClGQLAANYSSLQAISlEGNPAQKNVGDEQLRKYLLGLL 563
Cdd:cd00116  182 IRALAEglkancnLEVLDLNNNGLTDEGA-SALAETLASLKSLE-VLNLGDNNLTDAGAAALASALL 246
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 421-553 4.98e-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: 52.48  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 421 LRVLNLSGNAI----VRITAGALPRG--LHALNLSKNSI------SVIEGLRELTRLRVLDLSYNRI-----LRLGHGLA 483
Cdd:COG5238  182 VETVYLGCNQIgdegIEELAEALTQNttVTTLWLKRNPIgdegaeILAEALKGNKSLTTLDLSNNQIgdegvIALAEALK 261

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186511493 484 SCSSLKELYLAGNKISE------IEGLHRLLKLTVLDLRFNK--FSTTKCLGQLAANYSSLQAISLEGNpaqkNVGDE 553
Cdd:COG5238  262 NNTTVETLYLSGNQIGAegaialAKALQGNTTLTSLDLSVNRigDEGAIALAEGLQGNKTLHTLNLAYN----GIGAQ 335
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 421-521 9.65e-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: 51.71  E-value: 9.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 421 LRVLNLSGNAIVRITAGALPRGL------HALNLSKNSIS------VIEGLRELTRLRVLDLSYNRI-----LRLGHGLA 483
Cdd:COG5238  266 VETLYLSGNQIGAEGAIALAKALqgnttlTSLDLSVNRIGdegaiaLAEGLQGNKTLHTLNLAYNGIgaqgaIALAKALQ 345

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 186511493 484 SCSSLKELYLAGNKISEI--EGLHRLLK----LTVLDLRFNKFS 521
Cdd:COG5238  346 ENTTLHSLDLSDNQIGDEgaIALAKYLEgnttLRELNLGKNNIG 389
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 415-525 3.72e-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: 49.28  E-value: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 415 LSAFVGLRVLNLSGNAIVRITAGAL------PRGLHALNLSKNSISViEGLREL--------TRLRVLDLSYNRILRLGh 480
Cdd:cd00116  189 LKANCNLEVLDLNNNGLTDEGASALaetlasLKSLEVLNLGDNNLTD-AGAAALasallspnISLLTLSLSCNDITDDG- 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 186511493 481 glasCSSLKElYLAGNKIseieglhrllkLTVLDLRFNKFSTTKC 525
Cdd:cd00116  267 ----AKDLAE-VLAEKES-----------LLELDLRGNKFGEEGA 295
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 462-544 5.72e-06

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: 47.86  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 462 LTRLRVLDLSYNRILRLGhGLASCSSLKELYLAGNKISEIEGLHRLLKLTVLDLRFNKFSTTKCLGQLaanySSLQAISL 541
Cdd:cd21340    1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENL----VNLKKLYL 75


                 ...
gi 186511493 542 EGN 544
Cdd:cd21340   76 GGN 78
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 463-504 1.17e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 42.62  E-value: 1.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 186511493  463 TRLRVLDLSYNRILRLGhGLASCSSLKELYLAGN-KISEIEGL 504
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP-PLAKLPNLETLDLSGNnKITDLSDL 42
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 487-523 3.99e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.08  E-value: 3.99e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 186511493  487 SLKELYLAGNKISEIEGLHRLLKLTVLDLRFNKFSTT 523
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNNKITD 38
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 421-518 5.35e-05

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: 46.32  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 421 LRVLNLSGNAIVRITAGALPRGL------HALNLSKNSISV------IEGLRELTRLRVLDLSYNRI-----LRLGHGLA 483
Cdd:COG5238  294 LTSLDLSVNRIGDEGAIALAEGLqgnktlHTLNLAYNGIGAqgaialAKALQENTTLHSLDLSDNQIgdegaIALAKYLE 373

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 186511493 484 SCSSLKELYLAGNKISE--IEGLHRLLK---LTVLDLRFN 518
Cdd:COG5238  374 GNTTLRELNLGKNNIGKqgAEALIDALQtnrLHTLILDGN 413
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 421-544 1.08e-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: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 421 LRVLNLSGNAI----VRITAGALPRGLHALN---LSKNSISV------IEGLRELTRLRVLDLSYNRIL-----RLGHGL 482
Cdd:cd00116  110 LQELKLNNNGLgdrgLRLLAKGLKDLPPALEklvLGRNRLEGascealAKALRANRDLKELNLANNGIGdagirALAEGL 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511493 483 ASCSSLKELYLAGNKISEI------EGLHRLLKLTVLDLRFNKFS---TTKCLGQLAANYSSLQAISLEGN 544
Cdd:cd00116  190 KANCNLEVLDLNNNGLTDEgasalaETLASLKSLEVLNLGDNNLTdagAAALASALLSPNISLLTLSLSCN 260
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 443-477 1.27e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 39.92  E-value: 1.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 186511493  443 LHALNLSKNSISVIEGLRELTRLRVLDLSYNRILR 477
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNNKIT 37
PLN03150 PLN03150
hypothetical protein; Provisional
 415-475 1.19e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511493 415 LSAFVGLRVLNLSGNAI---VRITAGALPrGLHALNLSKNSI--SVIEGLRELTRLRVLDLSYNRI 475
Cdd:PLN03150 438 ISKLRHLQSINLSGNSIrgnIPPSLGSIT-SLEVLDLSYNSFngSIPESLGQLTSLRILNLNGNSL 502
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 421-490 1.72e-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: 41.19  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 421 LRVLNLSGNAIVRITAGAL-------PRGLHALNLSKNSI------SVIEGLRELTRLRVLDLSYNRILRLGHGLaSCSS 487
Cdd:cd00116  223 LEVLNLGDNNLTDAGAAALasallspNISLLTLSLSCNDItddgakDLAEVLAEKESLLELDLRGNKFGEEGAQL-LAES 301


                 ...
gi 186511493 488 LKE 490
Cdd:cd00116  302 LLE 304
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 421-565 2.11e-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: 40.80  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 421 LRVLNLSGNAIVRITAGALPRGLHA------LNLS--------KNSISVIEGLRELTRLRVLDLSYNRILRLG-HGLASC 485
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPqpslkeLCLSlnetgripRGLQSLLQGLTKGCGLQELDLSDNALGPDGcGVLESL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511493 486 ---SSLKELYLAGNKISE------IEGL-HRLLKLTVLDLRFNKFSTTKC--LGQLAANYSSLQAISLegnpAQKNVGDE 553
Cdd:cd00116  105 lrsSSLQELKLNNNGLGDrglrllAKGLkDLPPALEKLVLGRNRLEGASCeaLAKALRANRDLKELNL----ANNGIGDA 180

                        170
                 ....*....|..
gi 186511493 554 QLRKYLLGLLPN 565
Cdd:cd00116  181 GIRALAEGLKAN 192
PLN03150 PLN03150
hypothetical protein; Provisional
 441-499 3.45e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.57  E-value: 3.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186511493 441 RGLHALNLSKNSI--SVIEGLRELTRLRVLDLSYNRIL-RLGHGLASCSSLKELYLAGNKIS 499
Cdd:PLN03150 442 RHLQSINLSGNSIrgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS 503
 
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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