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Conserved domains on  [gi|124430564|ref|NP_038716|]
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dynein regulatory complex subunit 5 [Mus musculus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 10061432)

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
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 177-487 1.32e-86

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: 268.84  E-value: 1.32e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 177 DLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQ-LQTLVGGLKHLEELDlvYGVKDCGMNFE 255
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPsLKELCLSLNETGRIP--RGLQSLLQGLT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 256 --WNLFLFTYRDCYS---LAATIKACH---TLKIFKLTRSKVDDDKARILIRSLLDH-PALEELDLSHNLIGDRGARAAA 326
Cdd:cd00116   79 kgCGLQELDLSDNALgpdGCGVLESLLrssSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 327 KLLSH-SRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSE-PT 404
Cdd:cd00116  159 KALRAnRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 405 ATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHANREaaRQRTLNPGH 484
Cdd:cd00116  239 AALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN--ELESLWVKD 316


                 ...
gi 124430564 485 FSS 487
Cdd:cd00116  317 DSF 319
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 177-487 1.32e-86

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: 268.84  E-value: 1.32e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 177 DLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQ-LQTLVGGLKHLEELDlvYGVKDCGMNFE 255
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPsLKELCLSLNETGRIP--RGLQSLLQGLT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 256 --WNLFLFTYRDCYS---LAATIKACH---TLKIFKLTRSKVDDDKARILIRSLLDH-PALEELDLSHNLIGDRGARAAA 326
Cdd:cd00116   79 kgCGLQELDLSDNALgpdGCGVLESLLrssSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 327 KLLSH-SRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSE-PT 404
Cdd:cd00116  159 KALRAnRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 405 ATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHANREaaRQRTLNPGH 484
Cdd:cd00116  239 AALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN--ELESLWVKD 316


                 ...
gi 124430564 485 FSS 487
Cdd:cd00116  317 DSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 266-464 6.69e-35

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: 135.69  E-value: 6.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 266 CYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDRGARAAAKLLSH-SRLRVLNLANNQL 344
Cdd:COG5238  197 IEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNnTTVETLYLSGNQI 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 345 QAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLS 424
Cdd:COG5238  277 GAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLS 356

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 124430564 425 CNHIGQDGGKQLLEGISDNKTILEFDLRLSDVS-QESEYLI 464
Cdd:COG5238  357 DNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGkQGAEALI 397
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
304-331 3.81e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 3.81e-04
                           10        20
                   ....*....|....*....|....*...
gi 124430564   304 HPALEELDLSHNLIGDRGARAAAKLLSH 331
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
358-381 6.61e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 36.83  E-value: 6.61e-04
                          10        20
                  ....*....|....*....|....
gi 124430564  358 HNTNLVFLNLRLNCIEDEGGQAIA 381
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 177-487 1.32e-86

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: 268.84  E-value: 1.32e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 177 DLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQ-LQTLVGGLKHLEELDlvYGVKDCGMNFE 255
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPsLKELCLSLNETGRIP--RGLQSLLQGLT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 256 --WNLFLFTYRDCYS---LAATIKACH---TLKIFKLTRSKVDDDKARILIRSLLDH-PALEELDLSHNLIGDRGARAAA 326
Cdd:cd00116   79 kgCGLQELDLSDNALgpdGCGVLESLLrssSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 327 KLLSH-SRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSE-PT 404
Cdd:cd00116  159 KALRAnRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 405 ATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHANREaaRQRTLNPGH 484
Cdd:cd00116  239 AALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN--ELESLWVKD 316


                 ...
gi 124430564 485 FSS 487
Cdd:cd00116  317 DSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 266-464 6.69e-35

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: 135.69  E-value: 6.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 266 CYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDRGARAAAKLLSH-SRLRVLNLANNQL 344
Cdd:COG5238  197 IEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNnTTVETLYLSGNQI 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 345 QAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLS 424
Cdd:COG5238  277 GAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLS 356

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 124430564 425 CNHIGQDGGKQLLEGISDNKTILEFDLRLSDVS-QESEYLI 464
Cdd:COG5238  357 DNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGkQGAEALI 397
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 277-471 8.85e-30

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: 121.05  E-value: 8.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 277 HTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDRGARAAAKLLSHS-RLRVLNLANNQLQAPGAQSLAHA 355
Cdd:COG5238  180 NSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNkSLTTLDLSNNQIGDEGVIALAEA 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 356 LAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQ 435
Cdd:COG5238  260 LKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIA 339

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 124430564 436 LLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHAN 471
Cdd:COG5238  340 LAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGN 375
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 307-472 4.64e-27

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: 113.35  E-value: 4.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 307 LEELDLSHNLIGDRGARAAAK-LLSHSRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALE 385
Cdd:COG5238  182 VETVYLGCNQIGDEGIEELAEaLTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALK 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 386 TNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIG 465
Cdd:COG5238  262 NNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALA 341


                 ....*..
gi 124430564 466 QVLHANR 472
Cdd:COG5238  342 KALQENT 348
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 292-471 7.92e-21

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: 94.86  E-value: 7.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 292 DKARILIRSLLDHPALEELDLSHNL--IGDRGARAAAKLLSHSRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRL 369
Cdd:COG5238  138 PRRINLIQVLKDPLGGNAVHLLGLAarLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKR 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 370 NCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEF 449
Cdd:COG5238  218 NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL 297

                        170       180
                 ....*....|....*....|..
gi 124430564 450 DLRLSDVSQESEYLIGQVLHAN 471
Cdd:COG5238  298 DLSVNRIGDEGAIALAEGLQGN 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 231-358 5.76e-09

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: 58.26  E-value: 5.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 231 LVGGLKH---LEELDLVY-GVKDCGMNFewnlflftyrdcysLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPA 306
Cdd:COG5238  312 LAEGLQGnktLHTLNLAYnGIGAQGAIA--------------LAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTT 377

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124430564 307 LEELDLSHNLIGDRGARAAAKLLSHSRLRVLNLANNQLQAPGAQSLAHALAH 358
Cdd:COG5238  378 LRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGAEAQQRLEQLLER 429
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 311-484 4.51e-08

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: 55.18  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 311 DLSHNLIGDRGARAAAKLLSHSRLRVLNLANNQLQAPGAQsLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALE----- 385
Cdd:COG5238   93 DWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLI-LYLALPRRINLIQVLKDPLGGNAVHLLGLAARLGllaai 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 386 ------TNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQE 459
Cdd:COG5238  172 smakalQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDE 251

                        170       180
                 ....*....|....*....|....*
gi 124430564 460 SEYLIGQVLHANReaaRQRTLNPGH 484
Cdd:COG5238  252 GVIALAEALKNNT---TVETLYLSG 273
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
299-428 5.49e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.94  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 299 RSLLDHPALEELDLSHNLIGDRGARaaakLLSHSRLRVLNLANNQLqapgaQSLAHALAHNTNLVFLNLRLNCIEDeggq 378
Cdd:COG4886  107 EELSNLTNLESLDLSGNQLTDLPEE----LANLTNLKELDLSNNQL-----TDLPEPLGNLTNLKSLDLSNNQLTD---- 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 124430564 379 aIAHALETNKCLSVLHLGGNKLSEptatlLSQMLTVNTTLVSLNLSCNHI 428
Cdd:COG4886  174 -LPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQL 217
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
268-447 2.56e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.01  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 268 SLAATIKACHTLKIFKLTRSKVDDdkariLIRSLLDHPALEELDLSHNLIGDrgarAAAKLLSHSRLRVLNLANNQLqap 347
Cdd:COG4886  150 DLPEPLGNLTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQITD----LPEPLGNLTNLEELDLSGNQL--- 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 348 gaQSLAHALAHNTNLVFLNLRLNCIEDeggqaiAHALETNKCLSVLHLGGNKLSE-PTATLLSQmltvnttLVSLNLSCN 426
Cdd:COG4886  218 --TDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTDlPPLANLTN-------LKTLDLSNN 282

                        170       180
                 ....*....|....*....|.
gi 124430564 427 HIGQDGGKQLLEGISDNKTIL 447
Cdd:COG4886  283 QLTDLKLKELELLLGLNSLLL 303
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
253-428 3.98e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 253 NFEWNLFLFTYRDCYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNligdrgaraaAKLLSHS 332
Cdd:COG4886   44 SLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN----------EELSNLT 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 333 RLRVLNLANNQLqapgaQSLAHALAHNTNLVFLNLRLNCIEDeggqaIAHALETNKCLSVLHLGGNKLSEptatlLSQML 412
Cdd:COG4886  114 NLESLDLSGNQL-----TDLPEELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD-----LPEEL 178

                        170
                 ....*....|....*.
gi 124430564 413 TVNTTLVSLNLSCNHI 428
Cdd:COG4886  179 GNLTNLKELDLSNNQI 194
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
304-331 3.81e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 3.81e-04
                           10        20
                   ....*....|....*....|....*...
gi 124430564   304 HPALEELDLSHNLIGDRGARAAAKLLSH 331
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
358-381 6.61e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 36.83  E-value: 6.61e-04
                          10        20
                  ....*....|....*....|....
gi 124430564  358 HNTNLVFLNLRLNCIEDEGGQAIA 381
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
268-464 7.68e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 268 SLAATIKACHTLKIFKLTRSKVDDdkarilIRSLLDHPALEELDLSHNLIGDrgaraAAKLLSHSRLRVLNLANNQLQAP 347
Cdd:COG4886  219 DLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTD-----LPPLANLTNLKTLDLSNNQLTDL 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 348 GAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNH 427
Cdd:COG4886  288 KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLL 367

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 124430564 428 IGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLI 464
Cdd:COG4886  368 TLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLT 404
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
268-468 1.92e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 268 SLAATIKACHTLKIFKLTRSKVDDdkariLIRSLLDHPALEELDLSHNLIGDrgaraAAKLLSHSRLRVLNLANNQLQAP 347
Cdd:COG4886  196 DLPEPLGNLTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTD-----LPELGNLTNLEELDLSNNQLTDL 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 348 GAqslahaLAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNH 427
Cdd:COG4886  266 PP------LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTT 339

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 124430564 428 IGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVL 468
Cdd:COG4886  340 LALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLL 380
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 305-398 2.15e-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: 39.77  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124430564 305 PALEELDLSHN-------LIGDRGARAAaklLSHSrLRVLNLANNQLqapgaQSLAhALAHNTNLVFLNLRLNCIEDegG 377
Cdd:cd21340   90 TNLEELHIENQrlppgekLTFDPRSLAA---LSNS-LRVLNISGNNI-----DSLE-PLAPLRNLEQLDASNNQISD--L 157

                         90       100
                 ....*....|....*....|.
gi 124430564 378 QAIAHALETNKCLSVLHLGGN 398
Cdd:cd21340  158 EELLDLLSSWPSLRELDLTGN 178
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
331-358 2.61e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.46  E-value: 2.61e-03
                           10        20
                   ....*....|....*....|....*...
gi 124430564   331 HSRLRVLNLANNQLQAPGAQSLAHALAH 358
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
415-442 3.21e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 3.21e-03
                           10        20
                   ....*....|....*....|....*...
gi 124430564   415 NTTLVSLNLSCNHIGQDGGKQLLEGISD 442
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
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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