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Conserved domains on  [gi|568982030|ref|XP_006516836|]
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tubulin-specific chaperone E isoform X1 [Mus musculus]

Protein Classification

CAP_GLY and Ubl_TBCE domain-containing protein( domain architecture ID 13930791)

protein containing domains CAP_GLY, PPP1R42, and Ubl_TBCE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 379-461 1.72e-34

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.


:

Pssm-ID: 340564  Cd Length: 83  Bit Score: 123.84  E-value: 1.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 379 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 458
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568982030 459 LVR 461
Cdd:cd17044   81 LVR 83
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-67 6.03e-23

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 91.88  E-value: 6.03e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030    10 IGRRVEV--NGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCSQLRAL 67
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGI 60
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
88-284 1.60e-14

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.97  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  88 EACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGITwtEVLHCAPSW 167
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEEL---ANLTNLKELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLT--DLPEELGNL 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 168 PVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmF 245
Cdd:COG4886  182 TNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----L 249

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568982030 246 PALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLS 284
Cdd:COG4886  250 TNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 379-461 1.72e-34

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.


Pssm-ID: 340564  Cd Length: 83  Bit Score: 123.84  E-value: 1.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 379 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 458
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568982030 459 LVR 461
Cdd:cd17044   81 LVR 83
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-67 6.03e-23

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 91.88  E-value: 6.03e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030    10 IGRRVEV--NGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCSQLRAL 67
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGI 60
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-61 6.39e-21

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 85.92  E-value: 6.39e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568982030   10 IGRRVEVNGE-YATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKC 61
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFEC 52
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
88-284 1.60e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.97  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  88 EACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGITwtEVLHCAPSW 167
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEEL---ANLTNLKELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLT--DLPEELGNL 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 168 PVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmF 245
Cdd:COG4886  182 TNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----L 249

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568982030 246 PALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLS 284
Cdd:COG4886  250 TNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-61 8.18e-08

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 54.69  E-value: 8.18e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568982030  10 IGRRVEVNGEYATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKC 61
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHC 56
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 114-314 2.57e-07

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: 51.33  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 114 EQLKDLEALDLSENKLQFPSDSPTLTRtfstLKTLVLNKTGITWTEVLHCAPSwpvLEELYLKSNNISIserpVNVLQKM 193
Cdd:cd21340   21 SLCKNLKVLYLYDNKITKIENLEFLTN----LTHLYLQNNQIEKIENLENLVN---LKKLYLGGNRISV----VEGLENL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 194 RLL--------DLSSNPSIDESQLSLIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEWSFIN 265
Cdd:cd21340   90 TNLeelhienqRLPPGEKLTFDPRSLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQISDLEELL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568982030 266 E-LDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERR 314
Cdd:cd21340  162 DlLSSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
159-330 9.01e-06

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 45.91  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  159 EVLHCAPSW--PVLE-ELYLKSNNISISERPVNVLQKMRLLDLSSNpsiDESQLSLIADLPRLEHLVLSDIGLSSIHFPD 235
Cdd:pfam14580   7 ELIEQSAQYtnPVRErELDLRGYKIPIIENLGATLDQFDTIDFSDN---EIRKLDGFPLLRRLKTLLLNNNRICRIGEGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  236 AEIgcktsmFPALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRG 315
Cdd:pfam14580  84 GEA------LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQA 157

                         170
                  ....*....|....*
gi 568982030  316 AELDYRKAFGNEWRK 330
Cdd:pfam14580 158 AEKMFRSKQGKQLAK 172
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 381-456 3.98e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 38.78  E-value: 3.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982030   381 LTLKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEsskmpGREIElenDLQPLQFYSVENGD 456
Cdd:smart00213   1 IELTVKTLDGKTITL---EVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 59-284 8.19e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 38.68  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  59 FKCSQLRALQDISLWNCAVSHAGEQGRIAEACPNIRVVNLSKNLLStwDEVVLIAEQLKDLEALDLSENKLQFPSDSPTL 138
Cdd:PLN00113  37 FKSSINDPLKYLSNWNSSADVCLWQGITCNNSSRVVSIDLSGKNIS--GKISSAIFRLPYIQTINLSNNQLSGPIPDDIF 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 139 TrTFSTLKTLVLNKTGITWTevlhcAP--SWPVLEELYLkSNNISISERP--VNVLQKMRLLDLSSNPSIDESQLSlIAD 214
Cdd:PLN00113 115 T-TSSSLRYLNLSNNNFTGS-----IPrgSIPNLETLDL-SNNMLSGEIPndIGSFSSLKVLDLGGNVLVGKIPNS-LTN 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 215 LPRLEHLVLSDIGLSsihfpdAEIGCKTSMFPALKYLIVNDNQISEwSFINELDKLQSLQALSCTRNPLS 284
Cdd:PLN00113 187 LTSLEFLTLASNQLV------GQIPRELGQMKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLT 249
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 379-461 1.72e-34

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; TBCE, also termed tubulin-specific chaperone E, is a tubulin polymerizing protein involved in the second step of the tubulin folding pathway through cooperating in tubulin heterodimer dissociation both in vivo and in vitro. It may also be implicated in the maintenance of the neuronal microtubule network. Mutations in TBCE gene cause hypoparathyroidism, mental retardation and facial dysmorphism. TBCE contains an N-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain, a leucine-rich repeat protein-protein interaction domain followed by leucine-rich repeat (LRR) domains, and a C-terminal ubiquitin-like (Ubl) domain. Ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes.


Pssm-ID: 340564  Cd Length: 83  Bit Score: 123.84  E-value: 1.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 379 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 458
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568982030 459 LVR 461
Cdd:cd17044   81 LVR 83
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-67 6.03e-23

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 91.88  E-value: 6.03e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030    10 IGRRVEV--NGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCSQLRAL 67
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGI 60
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-61 6.39e-21

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 85.92  E-value: 6.39e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568982030   10 IGRRVEVNGE-YATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKC 61
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFEC 52
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
88-284 1.60e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.97  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  88 EACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGITwtEVLHCAPSW 167
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEEL---ANLTNLKELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLT--DLPEELGNL 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 168 PVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmF 245
Cdd:COG4886  182 TNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----L 249

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568982030 246 PALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLS 284
Cdd:COG4886  250 TNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
114-304 2.78e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 114 EQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGIT--WTEVLHCapswPVLEELYLKSNNISISERPVNVLQ 191
Cdd:COG4886  110 SNLTNLESLDLSGNQL---TDLPEELANLTNLKELDLSNNQLTdlPEPLGNL----TNLKSLDLSNNQLTDLPEELGNLT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 192 KMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpDAEIGcktsMFPALKYLIVNDNQISEwsfINELDK 269
Cdd:COG4886  183 NLKELDLSNNQitDLPEP----LGNLTNLEELDLSGNQLTDL---PEPLA----NLTNLETLDLSNNQLTD---LPELGN 248

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568982030 270 LQSLQALSCTRNPLSKADKaeeiiIAKIAQLRTLN 304
Cdd:COG4886  249 LTNLEELDLSNNQLTDLPP-----LANLTNLKTLD 278
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
62-299 2.77e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.95  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  62 SQLRALQDISLWNCAVSHAGEQgriAEACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLQ-FPSDSPTLTR 140
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEE---LANLTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTdLPEELGNLTN 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 141 tfstLKTLVLNKTGIT-WTEVLhcaPSWPVLEELYLKSNNISISERPVNVLQKMRLLDLSSNPsIdeSQLSLIADLPRLE 219
Cdd:COG4886  184 ----LKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQ-L--TDLPELGNLTNLE 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 220 HLVLSDIGLSSIHfpdaeigcKTSMFPALKYLIVNDNQISEWSfineLDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQ 299
Cdd:COG4886  254 ELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQLTDLK----LKELELLLGLNSLLLLLLLLNLLELLILLLLLT 321
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-61 8.18e-08

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 54.69  E-value: 8.18e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568982030  10 IGRRVEVNGEYATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKC 61
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHC 56
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 114-314 2.57e-07

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: 51.33  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 114 EQLKDLEALDLSENKLQFPSDSPTLTRtfstLKTLVLNKTGITWTEVLHCAPSwpvLEELYLKSNNISIserpVNVLQKM 193
Cdd:cd21340   21 SLCKNLKVLYLYDNKITKIENLEFLTN----LTHLYLQNNQIEKIENLENLVN---LKKLYLGGNRISV----VEGLENL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 194 RLL--------DLSSNPSIDESQLSLIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEWSFIN 265
Cdd:cd21340   90 TNLeelhienqRLPPGEKLTFDPRSLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQISDLEELL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 568982030 266 E-LDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERR 314
Cdd:cd21340  162 DlLSSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
96-304 3.70e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  96 VNLSKNLLSTWDEVVLIAEQLKDLEALDLSENKLQFPSDSPTLTRTFSTLKTLVLNKTGITWTEVLHCAPSWPVLEELYL 175
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 176 KSNNISISERPVNVLQKMRLLDLSSNPSIdesqlsliADLPRLEHLVLSDIGLSSIhfpDAEIGcktsMFPALKYLIVND 255
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGNEEL--------SNLTNLESLDLSGNQLTDL---PEELA----NLTNLKELDLSN 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568982030 256 NQISewSFINELDKLQSLQALSCTRNPLSKADKAeeiiIAKIAQLRTLN 304
Cdd:COG4886  146 NQLT--DLPEPLGNLTNLKSLDLSNNQLTDLPEE----LGNLTNLKELD 188
LRR_9 pfam14580
Leucine-rich repeat;
159-330 9.01e-06

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 45.91  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  159 EVLHCAPSW--PVLE-ELYLKSNNISISERPVNVLQKMRLLDLSSNpsiDESQLSLIADLPRLEHLVLSDIGLSSIHFPD 235
Cdd:pfam14580   7 ELIEQSAQYtnPVRErELDLRGYKIPIIENLGATLDQFDTIDFSDN---EIRKLDGFPLLRRLKTLLLNNNRICRIGEGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  236 AEIgcktsmFPALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRG 315
Cdd:pfam14580  84 GEA------LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQA 157

                         170
                  ....*....|....*
gi 568982030  316 AELDYRKAFGNEWRK 330
Cdd:pfam14580 158 AEKMFRSKQGKQLAK 172
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 383-461 1.62e-04

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 39.89  E-value: 1.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568982030 383 LKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYesskmpgREIELENDlQPLQFYSVENGDCLLVR 461
Cdd:cd17039    1 ITVKTLDGKTYTV---EVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 61-224 2.37e-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: 43.11  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  61 CSQLRALQDISLWNCAVSHAGEQgRIAEA----CPNIRVVNLSKNLLSTWDEVVLiAEQLK---DLEALDLSENKLQfPS 133
Cdd:cd00116  104 LLRSSSLQELKLNNNGLGDRGLR-LLAKGlkdlPPALEKLVLGRNRLEGASCEAL-AKALRanrDLKELNLANNGIG-DA 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 134 DSPTLTRTF---STLKTLVLNKTGITWTEVL---HCAPSWPVLEELYLKSNNIS------ISERPVNVLQKMRLLDLSSN 201
Cdd:cd00116  181 GIRALAEGLkanCNLEVLDLNNNGLTDEGASalaETLASLKSLEVLNLGDNNLTdagaaaLASALLSPNISLLTLSLSCN 260

                        170       180
                 ....*....|....*....|....*.
gi 568982030 202 PSIDESQLSL---IADLPRLEHLVLS 224
Cdd:cd00116  261 DITDDGAKDLaevLAEKESLLELDLR 286
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 381-456 3.98e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 38.78  E-value: 3.98e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568982030   381 LTLKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEsskmpGREIElenDLQPLQFYSVENGD 456
Cdd:smart00213   1 IELTVKTLDGKTITL---EVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 81-212 1.15e-03

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 41.31  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  81 GEQG--RIAEA---CPNIRVVNLSKNLLSTwDEVVLIAEQLKD---LEALDLSENKLQFPSDS--PTLTRTFSTLKTLVL 150
Cdd:COG5238  221 GDEGaeILAEAlkgNKSLTTLDLSNNQIGD-EGVIALAEALKNnttVETLYLSGNQIGAEGAIalAKALQGNTTLTSLDL 299

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 151 NKTGITWTEVLHCAPSWPV---LEELYLKSNNISIS--ERPVNVLQKMR---LLDLSSNPSIDESQLSLI 212
Cdd:COG5238  300 SVNRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAQgaIALAKALQENTtlhSLDLSDNQIGDEGAIALA 369
Ubl_IQUB cd17061
ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) ...
 382-433 5.44e-03

ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) and similar proteins; IQUB is an IQ motif and ubiquitin domain-containing protein that may play roles in cilia formation and/or maintenance. It contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340581  Cd Length: 79  Bit Score: 35.70  E-value: 5.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568982030 382 TLKIKCsnQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKM 433
Cdd:cd17061    4 TVKFVL--MPSGQVITLAFTLGQTIGELKEHFSSELKIPPDVLQIMFDGKLV 53
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 59-284 8.19e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 38.68  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030  59 FKCSQLRALQDISLWNCAVSHAGEQGRIAEACPNIRVVNLSKNLLStwDEVVLIAEQLKDLEALDLSENKLQFPSDSPTL 138
Cdd:PLN00113  37 FKSSINDPLKYLSNWNSSADVCLWQGITCNNSSRVVSIDLSGKNIS--GKISSAIFRLPYIQTINLSNNQLSGPIPDDIF 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 139 TrTFSTLKTLVLNKTGITWTevlhcAP--SWPVLEELYLkSNNISISERP--VNVLQKMRLLDLSSNPSIDESQLSlIAD 214
Cdd:PLN00113 115 T-TSSSLRYLNLSNNNFTGS-----IPrgSIPNLETLDL-SNNMLSGEIPndIGSFSSLKVLDLGGNVLVGKIPNS-LTN 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568982030 215 LPRLEHLVLSDIGLSsihfpdAEIGCKTSMFPALKYLIVNDNQISEwSFINELDKLQSLQALSCTRNPLS 284
Cdd:PLN00113 187 LTSLEFLTLASNQLV------GQIPRELGQMKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLT 249
 
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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