NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17541264|ref|NP_501395|]
View 

Tubulin-specific chaperone E [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 3-65 1.20e-20

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: 85.53  E-value: 1.20e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541264     3 IGQRVRINFE-VATVRYIGEVDGyGSQRWVGLEWDDPtRGKHDGIVRGKRYFQTRhPNGGSLMK 65
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPF-APGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVR 61
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 410-491 2.06e-17

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: 76.85  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 410 AVVKIRIECGN----RVETRRLPLGMSIQKIRDMLARLFKVPnTSKIRLYLVMSEKAKQHrIELENPLREFGHYSPsEDR 485
Cdd:cd17044   1 SLITLTLVCPAapekKPIEKKLPSSMTVQKLKGLCERLFKLP-ASKQRLSYVSSEGPGIE-IELDDDLRSLSFYSV-EDG 77


                ....*.
gi 17541264 486 DILVVE 491
Cdd:cd17044  78 DTILVR 83
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
73-336 1.35e-10

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


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264  73 TDLLFEIKDRYIEEESVETEIELAQSNKKIELIGMDQTAAKQSNIEKLINIVLDNRSVGFPPSsdspQFILCRELNLYGN 152
Cdd:COG4886  48 LLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS----NLTNLESLDLSGN 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 153 LLykwKTVRQILEYFPRIQELNLRRNRMQCFNEEEDddesegddhvysdSCKKLviSECNLSENSIDSI---LLRFPSTS 229
Cdd:COG4886 124 QL---TDLPEELANLTNLKELDLSNNQLTDLPEPLG-------------NLTNL--KSLDLSNNQLTDLpeeLGNLTNLK 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 230 DVVAFGNDLTRFSVSEAVSSRLTSLDLEDNPFKTLDSIHGTFPNLTQLSVANCGITSLNGFDgsiKFPKLEYLNIKRNSI 309
Cdd:COG4886 186 ELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELG---NLTNLEELDLSNNQL 262

                       250       260
                ....*....|....*....|....*..
gi 17541264 310 vewKSVNSIRSLKSLKRLLFDCKKLST 336
Cdd:COG4886 263 ---TDLPPLANLTNLKTLDLSNNQLTD 286
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 3-65 1.20e-20

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: 85.53  E-value: 1.20e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541264     3 IGQRVRINFE-VATVRYIGEVDGyGSQRWVGLEWDDPtRGKHDGIVRGKRYFQTRhPNGGSLMK 65
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPF-APGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVR 61
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 3-65 1.22e-20

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: 85.33  E-value: 1.22e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541264      3 IGQRVRI--NFEVATVRYIGEVDGYGSQrWVGLEWDDPTRGKHDGIVRGKRYFQTRhPNGGSLMK 65
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGV-WVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVR 63
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 410-491 2.06e-17

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: 76.85  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 410 AVVKIRIECGN----RVETRRLPLGMSIQKIRDMLARLFKVPnTSKIRLYLVMSEKAKQHrIELENPLREFGHYSPsEDR 485
Cdd:cd17044   1 SLITLTLVCPAapekKPIEKKLPSSMTVQKLKGLCERLFKLP-ASKQRLSYVSSEGPGIE-IELDDDLRSLSFYSV-EDG 77


                ....*.
gi 17541264 486 DILVVE 491
Cdd:cd17044  78 DTILVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
73-336 1.35e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264  73 TDLLFEIKDRYIEEESVETEIELAQSNKKIELIGMDQTAAKQSNIEKLINIVLDNRSVGFPPSsdspQFILCRELNLYGN 152
Cdd:COG4886  48 LLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS----NLTNLESLDLSGN 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 153 LLykwKTVRQILEYFPRIQELNLRRNRMQCFNEEEDddesegddhvysdSCKKLviSECNLSENSIDSI---LLRFPSTS 229
Cdd:COG4886 124 QL---TDLPEELANLTNLKELDLSNNQLTDLPEPLG-------------NLTNL--KSLDLSNNQLTDLpeeLGNLTNLK 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 230 DVVAFGNDLTRFSVSEAVSSRLTSLDLEDNPFKTLDSIHGTFPNLTQLSVANCGITSLNGFDgsiKFPKLEYLNIKRNSI 309
Cdd:COG4886 186 ELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELG---NLTNLEELDLSNNQL 262

                       250       260
                ....*....|....*....|....*..
gi 17541264 310 vewKSVNSIRSLKSLKRLLFDCKKLST 336
Cdd:COG4886 263 ---TDLPPLANLTNLKTLDLSNNQLTD 286
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 1-53 6.63e-07

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: 51.99  E-value: 6.63e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17541264   1 MEIGQRVRINFEVATVRYIGEVDgYGSQRWVGLEWDDPtRGKHDGIVRGKRYF 53
Cdd:COG5244   4 LSVNDRVLLGDKFGTVRFIGKTK-FKDGIWIGLELDDP-VGKNDGSVNGVRYF 54
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 265-367 1.06e-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: 40.54  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 265 DSIHGTFPNLTQLSVANCGITSLNGFDGsikFPKLEYLNIKRNSIVEWKSV-NSIRSLKSLKRLlfDCKKLSTEKGVHAY 343
Cdd:cd21340 113 RSLAALSNSLRVLNISGNNIDSLEPLAP---LRNLEQLDASNNQISDLEELlDLLSSWPSLREL--DLTGNPVCKKPKYR 187

                        90       100
                ....*....|....*....|....
gi 17541264 344 EIVIAKLSTLIDLNRFDVSEVERR 367
Cdd:cd21340 188 DKIILASKSLEVLDGKEITDTERQ 211
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 3-65 1.20e-20

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: 85.53  E-value: 1.20e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17541264     3 IGQRVRINFE-VATVRYIGEVDGyGSQRWVGLEWDDPtRGKHDGIVRGKRYFQTRhPNGGSLMK 65
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPF-APGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVR 61
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 3-65 1.22e-20

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: 85.33  E-value: 1.22e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17541264      3 IGQRVRI--NFEVATVRYIGEVDGYGSQrWVGLEWDDPTRGKHDGIVRGKRYFQTRhPNGGSLMK 65
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGV-WVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVR 63
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 410-491 2.06e-17

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: 76.85  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 410 AVVKIRIECGN----RVETRRLPLGMSIQKIRDMLARLFKVPnTSKIRLYLVMSEKAKQHrIELENPLREFGHYSPsEDR 485
Cdd:cd17044   1 SLITLTLVCPAapekKPIEKKLPSSMTVQKLKGLCERLFKLP-ASKQRLSYVSSEGPGIE-IELDDDLRSLSFYSV-EDG 77


                ....*.
gi 17541264 486 DILVVE 491
Cdd:cd17044  78 DTILVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
73-336 1.35e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264  73 TDLLFEIKDRYIEEESVETEIELAQSNKKIELIGMDQTAAKQSNIEKLINIVLDNRSVGFPPSsdspQFILCRELNLYGN 152
Cdd:COG4886  48 LLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS----NLTNLESLDLSGN 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 153 LLykwKTVRQILEYFPRIQELNLRRNRMQCFNEEEDddesegddhvysdSCKKLviSECNLSENSIDSI---LLRFPSTS 229
Cdd:COG4886 124 QL---TDLPEELANLTNLKELDLSNNQLTDLPEPLG-------------NLTNL--KSLDLSNNQLTDLpeeLGNLTNLK 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 230 DVVAFGNDLTRFSVSEAVSSRLTSLDLEDNPFKTLDSIHGTFPNLTQLSVANCGITSLNGFDgsiKFPKLEYLNIKRNSI 309
Cdd:COG4886 186 ELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELG---NLTNLEELDLSNNQL 262

                       250       260
                ....*....|....*....|....*..
gi 17541264 310 vewKSVNSIRSLKSLKRLLFDCKKLST 336
Cdd:COG4886 263 ---TDLPPLANLTNLKTLDLSNNQLTD 286
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-404 1.29e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.78  E-value: 1.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 145 RELNLYGNLLykwKTVRQILEYFPRIQELNLRRNRMQCFNEEEdddesegddhvysDSCKKLviSECNLSENSIDSI--- 221
Cdd:COG4886 139 KELDLSNNQL---TDLPEPLGNLTNLKSLDLSNNQLTDLPEEL-------------GNLTNL--KELDLSNNQITDLpep 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 222 LLRFPSTSDVVAFGNDLTRFSVSEAVSSRLTSLDLEDNPFKTLDSIhGTFPNLTQLSVANCGITSLngfDGSIKFPKLEY 301
Cdd:COG4886 201 LGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPEL-GNLTNLEELDLSNNQLTDL---PPLANLTNLKT 276

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 302 LNIKRNSIvewksvnSIRSLKSLKRLLFDCKKLSTEKGVHAYEIVIAKLSTLIDLNRFDVSEVERRSAEIRFLNKYAGLN 381
Cdd:COG4886 277 LDLSNNQL-------TDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLAL 349

                       250       260
                ....*....|....*....|...
gi 17541264 382 DNEDHQDDIKRLIEIHGEPTLDT 404
Cdd:COG4886 350 LTLLLLLNLLSLLLTLLLTLGLL 372
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
235-357 3.16e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 3.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 235 GNDLTRFSVSEAVSSRLTSLDLEDNPFKTLDSIHGTFPNLTQLSVANCGITSLNGFDGSIkfPKLEYLNIKRNSIVEWKS 314
Cdd:COG4886 122 GNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNL--TNLKELDLSNNQITDLPE 199

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17541264 315 vnSIRSLKSLKRLLFDCKKLSTekgvhaYEIVIAKLSTLIDLN 357
Cdd:COG4886 200 --PLGNLTNLEELDLSGNQLTD------LPEPLANLTNLETLD 234
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 1-53 6.63e-07

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: 51.99  E-value: 6.63e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17541264   1 MEIGQRVRINFEVATVRYIGEVDgYGSQRWVGLEWDDPtRGKHDGIVRGKRYF 53
Cdd:COG5244   4 LSVNDRVLLGDKFGTVRFIGKTK-FKDGIWIGLELDDP-VGKNDGSVNGVRYF 54
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
249-357 6.91e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 6.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 249 SRLTSLDLEDNPFKTLDSIHGTFPNLTQLSVANCGITSLngfDGSI-KFPKLEYLNIKRNSIvewKSV-NSIRSLKSLKR 326
Cdd:COG4886 113 TNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDL---PEPLgNLTNLKSLDLSNNQL---TDLpEELGNLTNLKE 186

                        90       100       110
                ....*....|....*....|....*....|.
gi 17541264 327 LLFDCKKLSTEKGvhayeiVIAKLSTLIDLN 357
Cdd:COG4886 187 LDLSNNQITDLPE------PLGNLTNLEELD 211
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 265-367 1.06e-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: 40.54  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 265 DSIHGTFPNLTQLSVANCGITSLNGFDGsikFPKLEYLNIKRNSIVEWKSV-NSIRSLKSLKRLlfDCKKLSTEKGVHAY 343
Cdd:cd21340 113 RSLAALSNSLRVLNISGNNIDSLEPLAP---LRNLEQLDASNNQISDLEELlDLLSSWPSLREL--DLTGNPVCKKPKYR 187

                        90       100
                ....*....|....*....|....
gi 17541264 344 EIVIAKLSTLIDLNRFDVSEVERR 367
Cdd:cd21340 188 DKIILASKSLEVLDGKEITDTERQ 211
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 204-372 5.18e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 38.88  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 204 KKLVISECNLSENSIDSILLRFPSTSDvvafgndltrfsvseavssrLTSLDLEDNP-----FKTLDSIHGTFPNLTQLS 278
Cdd:cd00116 140 EKLVLGRNRLEGASCEALAKALRANRD--------------------LKELNLANNGigdagIRALAEGLKANCNLEVLD 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 279 VANCGITSLNGFDGSIKFP---KLEYLNIKRNSIVEW---KSVNSIRSL-KSLKRLLFDCKKLsTEKGVHAYEIVIAKLS 351
Cdd:cd00116 200 LNNNGLTDEGASALAETLAslkSLEVLNLGDNNLTDAgaaALASALLSPnISLLTLSLSCNDI-TDDGAKDLAEVLAEKE 278

                       170       180
                ....*....|....*....|....
gi 17541264 352 TL--IDLNRFDVS-EVERRSAEIR 372
Cdd:cd00116 279 SLleLDLRGNKFGeEGAQLLAESL 302
Ubl_TBCEL cd17045
ubiquitin-like (Ubl) domain found in tubulin-specific chaperone cofactor E-like protein (TBCEL) ...
 411-491 5.65e-03

ubiquitin-like (Ubl) domain found in tubulin-specific chaperone cofactor E-like protein (TBCEL) and similar proteins; TBCEL, also termed leucine-rich repeat-containing protein 35 (LRRC35), or E-like (EL), is a novel regulator of tubulin stability, suggesting a link between tubulin turnover and vesicle transport. TBCEL is abundantly expressed in testis, but is also present in several tissues at a much lower level. It is required for the synchronous movement of the investment cones and is important for normal male fertility. TBCEL shows high sequence similarity to tubulin-specific chaperone cofactor E (TBCE), a component of the multimolecular complex required for tubulin heterodimer formation in all eukaryotic cells. It contains a leucine-rich repeat protein-protein interaction domain and a C-terminal ubiquitin-like (Ubl) domain, but does not harbor the cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain found in TBCE.


Pssm-ID: 340565  Cd Length: 87  Bit Score: 36.07  E-value: 5.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541264 411 VVKIRIECGNRVETRRLPLGMSIQKIRDMLARLFKVPnTSKIRLYLVMSEKAKQHRIELENPLREFGHYSPSEDRDILVV 490
Cdd:cd17045   7 SAKVTVHFEDQVESMDIDLDQTVAELKKQLKNLVGLP-PSKMRLYYIDIEMSIFGPEELRFPSRALYSYNIRDGDEILVE 85


                .
gi 17541264 491 E 491
Cdd:cd17045  86 P 86
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH