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Conserved domains on  [gi|31543843|ref|NP_848027|]
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tubulin-specific chaperone E [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; ...
 441-523 3.70e-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: 3.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 441 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 520
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                ...
gi 31543843 521 LVR 523
Cdd:cd17044  81 LVR 83
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-75 3.85e-28

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: 106.52  E-value: 3.85e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543843     10 IGRRVEV--NGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCRhPTGGSFVRPSKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
150-346 2.50e-15

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.05  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 150 EACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGITwtEVLHCAPSW 229
Cdd:COG4886 110 SNLTNLESLDLSGNQLTDLPEEL---ANLTNLKELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLT--DLPEELGNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 230 PVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmF 307
Cdd:COG4886 182 TNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----L 249

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31543843 308 PALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLS 346
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; ...
 441-523 3.70e-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: 3.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 441 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 520
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                ...
gi 31543843 521 LVR 523
Cdd:cd17044  81 LVR 83
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-75 3.85e-28

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: 106.52  E-value: 3.85e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543843     10 IGRRVEV--NGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCRhPTGGSFVRPSKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 3.31e-27

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: 104.02  E-value: 3.31e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543843    10 IGRRVEVNGE-YATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKCRhPTGGSFVRPSKV 75
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
150-346 2.50e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.05  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 150 EACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGITwtEVLHCAPSW 229
Cdd:COG4886 110 SNLTNLESLDLSGNQLTDLPEEL---ANLTNLKELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLT--DLPEELGNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 230 PVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmF 307
Cdd:COG4886 182 TNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----L 249

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31543843 308 PALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLS 346
Cdd:COG4886 250 TNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 2.03e-09

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: 60.08  E-value: 2.03e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543843  10 IGRRVEVNGEYATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKCRHPTgGSFVRPSKVN 76
Cdd:COG5244   6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 207-376 1.42e-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: 52.10  E-value: 1.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 207 LKTLVL--NKtgITWTEVLHCAPSwpvLEELYLKSNNISISErPVNVLQKMRLLDLSSN-----------PSIDESQL-- 271
Cdd:cd21340  26 LKVLYLydNK--ITKIENLEFLTN---LTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNrisvveglenlTNLEELHIen 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 272 --------------SLIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEWSFINE-LDKLQSLQ 336
Cdd:cd21340 100 qrlppgekltfdprSLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQISDLEELLDlLSSWPSLR 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 31543843 337 ALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERR 376
Cdd:cd21340 172 ELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
221-392 7.58e-06

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 46.30  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843   221 EVLHCAPSW--PVLE-ELYLKSNNISISERPVNVLQKMRLLDLSSNpsiDESQLSLIADLPRLEHLVLSDIGLSSIHFPD 297
Cdd:pfam14580   7 ELIEQSAQYtnPVRErELDLRGYKIPIIENLGATLDQFDTIDFSDN---EIRKLDGFPLLRRLKTLLLNNNRICRIGEGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843   298 AEIgcktsmFPALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRG 377
Cdd:pfam14580  84 GEA------LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQA 157

                         170
                  ....*....|....*
gi 31543843   378 AELDYRKAFGNEWRK 392
Cdd:pfam14580 158 AEKMFRSKQGKQLAK 172
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 443-518 5.64e-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: 38.39  E-value: 5.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543843    443 LTLKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEsskmpGREIElenDLQPLQFYSVENGD 518
Cdd:smart00213   1 IELTVKTLDGKTITL---EVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 441-523 3.70e-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: 3.70e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 441 QLLTLKIKCSNQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKMPGREIELENDLQPLQFYSVENGDCL 520
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                ...
gi 31543843 521 LVR 523
Cdd:cd17044  81 LVR 83
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-75 3.85e-28

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: 106.52  E-value: 3.85e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31543843     10 IGRRVEV--NGEYATVRFCGAVPPVAGLWLGVEWDNPERGKHDGSHEGTMYFKCRhPTGGSFVRPSKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 3.31e-27

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: 104.02  E-value: 3.31e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543843    10 IGRRVEVNGE-YATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKCRhPTGGSFVRPSKV 75
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
150-346 2.50e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.05  E-value: 2.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 150 EACPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLqfpSDSPTLTRTFSTLKTLVLNKTGITwtEVLHCAPSW 229
Cdd:COG4886 110 SNLTNLESLDLSGNQLTDLPEEL---ANLTNLKELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLT--DLPEELGNL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 230 PVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmF 307
Cdd:COG4886 182 TNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltDLPEP----LANLTNLETLDLSNNQLTDL----PELGN----L 249

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 31543843 308 PALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLS 346
Cdd:COG4886 250 TNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
119-366 2.64e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.89  E-value: 2.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 119 ITKKQSQLRALQDISLWNCAVSHAGEQGRIAEACPNIRVVNLSKNLLStwdevvliaEQLKDLEALDLSENKLqfpSDSP 198
Cdd:COG4886  62 LSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQL---TDLP 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 199 TLTRTFSTLKTLVLNKTGIT--WTEVLHCapswPVLEELYLKSNNISISERPVNVLQKMRLLDLSSNP--SIDESqlslI 274
Cdd:COG4886 130 EELANLTNLKELDLSNNQLTdlPEPLGNL----TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQitDLPEP----L 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 275 ADLPRLEHLVLSDIGLSSIhfpDAEIGcktsMFPALKYLIVNDNQISEwsfINELDKLQSLQALSCTRNPLSKADKaeei 354
Cdd:COG4886 202 GNLTNLEELDLSGNQLTDL---PEPLA----NLTNLETLDLSNNQLTD---LPELGNLTNLEELDLSNNQLTDLPP---- 267

                       250
                ....*....|..
gi 31543843 355 iIAKIAQLRTLN 366
Cdd:COG4886 268 -LANLTNLKTLD 278
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-361 4.14e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.04  E-value: 4.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 124 SQLRALQDISLWNCAVSHAGEQgrIAEaCPNIRVVNLSKNLLSTWDEVVliaEQLKDLEALDLSENKLQ-FPSDSPTLTR 202
Cdd:COG4886 110 SNLTNLESLDLSGNQLTDLPEE--LAN-LTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTdLPEELGNLTN 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 203 tfstLKTLVLNKTGIT-WTEVLhcaPSWPVLEELYLKSNNISISERPVNVLQKMRLLDLSSNPsIdeSQLSLIADLPRLE 281
Cdd:COG4886 184 ----LKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQ-L--TDLPELGNLTNLE 253

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 282 HLVLSDIGLSSIHfpdaeigcKTSMFPALKYLIVNDNQISEWSfineLDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQ 361
Cdd:COG4886 254 ELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQLTDLK----LKELELLLGLNSLLLLLLLLNLLELLILLLLLT 321
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 2.03e-09

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: 60.08  E-value: 2.03e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31543843  10 IGRRVEVNGEYATVRFCGAVPPVAGLWLGVEWDNPeRGKHDGSHEGTMYFKCRHPTgGSFVRPSKVN 76
Cdd:COG5244   6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 207-376 1.42e-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: 52.10  E-value: 1.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 207 LKTLVL--NKtgITWTEVLHCAPSwpvLEELYLKSNNISISErPVNVLQKMRLLDLSSN-----------PSIDESQL-- 271
Cdd:cd21340  26 LKVLYLydNK--ITKIENLEFLTN---LTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNrisvveglenlTNLEELHIen 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 272 --------------SLIADLPRLEHLVLSDIGLSSIhfpdAEIGCktsmFPALKYLIVNDNQISEWSFINE-LDKLQSLQ 336
Cdd:cd21340 100 qrlppgekltfdprSLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQISDLEELLDlLSSWPSLR 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 31543843 337 ALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERR 376
Cdd:cd21340 172 ELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
158-366 1.19e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 158 VNLSKNLLSTWDEVVLIAEQLKDLEALDLSENKLQFPSDSPTLTRTFSTLKTLVLNKTGITWTEVLHCAPSWPVLEELYL 237
Cdd:COG4886   1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 238 KSNNISISERPVNVLQKMRLLDLSSNPSIdesqlsliADLPRLEHLVLSDIGLSSIhfpDAEIGcktsMFPALKYLIVND 317
Cdd:COG4886  81 LLSLLLLGLTDLGDLTNLTELDLSGNEEL--------SNLTNLESLDLSGNQLTDL---PEELA----NLTNLKELDLSN 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 31543843 318 NQISewSFINELDKLQSLQALSCTRNPLSKADKAeeiiIAKIAQLRTLN 366
Cdd:COG4886 146 NQLT--DLPEPLGNLTNLKSLDLSNNQLTDLPEE----LGNLTNLKELD 188
LRR_9 pfam14580
Leucine-rich repeat;
221-392 7.58e-06

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 46.30  E-value: 7.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843   221 EVLHCAPSW--PVLE-ELYLKSNNISISERPVNVLQKMRLLDLSSNpsiDESQLSLIADLPRLEHLVLSDIGLSSIHFPD 297
Cdd:pfam14580   7 ELIEQSAQYtnPVRErELDLRGYKIPIIENLGATLDQFDTIDFSDN---EIRKLDGFPLLRRLKTLLLNNNRICRIGEGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843   298 AEIgcktsmFPALKYLIVNDNQISEWSFINELDKLQSLQALSCTRNPLSKADKAEEIIIAKIAQLRTLNRCQILPEERRG 377
Cdd:pfam14580  84 GEA------LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQA 157

                         170
                  ....*....|....*
gi 31543843   378 AELDYRKAFGNEWRK 392
Cdd:pfam14580 158 AEKMFRSKQGKQLAK 172
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 98-274 2.00e-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: 47.09  E-value: 2.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843  98 DENSCSLKVGSKQVQTIGFEHITKKQSQLRALQDISLWNcavSHAGEQG--RIAEA---CPNIRVVNLSKNLLSTwDEVV 172
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKR---NPIGDEGaeILAEAlkgNKSLTTLDLSNNQIGD-EGVI 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 173 LIAEQLKD---LEALDLSENKLQFPSDS--PTLTRTFSTLKTLVLNKTGITWTEVLHCAPSWPV---LEELYLKSNNISI 244
Cdd:COG5238 255 ALAEALKNnttVETLYLSGNQIGAEGAIalAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGnktLHTLNLAYNGIGA 334

                       170       180       190
                ....*....|....*....|....*....|....*
gi 31543843 245 S--ERPVNVLQKMR---LLDLSSNPSIDESQLSLI 274
Cdd:COG5238 335 QgaIALAKALQENTtlhSLDLSDNQIGDEGAIALA 369
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 445-523 2.27e-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: 39.50  E-value: 2.27e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31543843 445 LKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYesskmpgREIELENDlQPLQFYSVENGDCLLVR 523
Cdd:cd17039   1 ITVKTLDGKTYTV---EVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 129-286 3.03e-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: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 129 LQDISLWNCAVSHAGEQgRIAEA----CPNIRVVNLSKNLLSTWDEVVLiAEQLK---DLEALDLSENKLQfPSDSPTLT 201
Cdd:cd00116 110 LQELKLNNNGLGDRGLR-LLAKGlkdlPPALEKLVLGRNRLEGASCEAL-AKALRanrDLKELNLANNGIG-DAGIRALA 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543843 202 RTF---STLKTLVLNKTGITWTEVL---HCAPSWPVLEELYLKSNNIS------ISERPVNVLQKMRLLDLSSNPSIDES 269
Cdd:cd00116 187 EGLkanCNLEVLDLNNNGLTDEGASalaETLASLKSLEVLNLGDNNLTdagaaaLASALLSPNISLLTLSLSCNDITDDG 266

                       170       180
                ....*....|....*....|
gi 31543843 270 QLSL---IADLPRLEHLVLS 286
Cdd:cd00116 267 AKDLaevLAEKESLLELDLR 286
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 443-518 5.64e-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: 38.39  E-value: 5.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31543843    443 LTLKIKCSNQPERQIlekQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEsskmpGREIElenDLQPLQFYSVENGD 518
Cdd:smart00213   1 IELTVKTLDGKTITL---EVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
Ubl_IQUB cd17061
ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) ...
 444-495 6.28e-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: 6.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 31543843 444 TLKIKCsnQPERQILEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESSKM 495
Cdd:cd17061   4 TVKFVL--MPSGQVITLAFTLGQTIGELKEHFSSELKIPPDVLQIMFDGKLV 53
 
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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