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Conserved domains on  [gi|442622399|ref|NP_610197|]
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Tubulin-specific chaperone E, isoform C [Drosophila melanogaster]

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
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 14-79 3.38e-25

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: 98.43  E-value: 3.38e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622399    14 LGTRIKIGDN--YGTVRYVGEVSGHMGSWLGIEWDDGLRGKHNGIVDGKRYFQTQtPTGGSFIRPGKV 79
Cdd:smart01052   1 VGDRVEVGGGgrRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 443-523 2.14e-24

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: 96.88  E-value: 2.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 443 NLINVSIRHQL--TGETWEKKVPRMITVQTLQGLVMKRFRLSGDVPQLCYVDALHPDLVVPLDNNAKTLDFYSVQEHDTV 520
Cdd:cd17044    1 SLITLTLVCPAapEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 442622399 521 LVQ 523
Cdd:cd17044   81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
131-376 3.50e-13

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 131 SKFEQLEEVSVDQTPVNAAGY-LKELTHLTTLNVSHTLIwnWEIVASIAqQLPSLTNLNLSSNRL-VLP----------- 197
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQL--TDLPEPLG-NLTNLKSLDLSNNQLtDLPeelgnltnlke 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 198 ---TSSQITELEPSF---RQLKRINLRSCGFSDWKDVMHTallWPNILSLGLQENSLGQLAEVDRtkiFKQLHELDLHRT 271
Cdd:COG4886  187 ldlSNNQITDLPEPLgnlTNLEELDLSGNQLTDLPEPLAN---LTNLETLDLSNNQLTDLPELGN---LTNLEELDLSNN 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 272 NIMDFDqvtKLGNLTTLRLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQLNLLHNPIWNEADAFNELDKLPQLKRLSKTP 351
Cdd:COG4886  261 QLTDLP---PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTL 337

                        250       260
                 ....*....|....*....|....*
gi 442622399 352 HLKSNFDEMFSKAVASIASLQFINK 376
Cdd:COG4886  338 TTLALSLSLLALLTLLLLLNLLSLL 362
 
Name Accession Description Interval E-value
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 14-79 3.38e-25

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: 98.43  E-value: 3.38e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622399    14 LGTRIKIGDN--YGTVRYVGEVSGHMGSWLGIEWDDGLRGKHNGIVDGKRYFQTQtPTGGSFIRPGKV 79
Cdd:smart01052   1 VGDRVEVGGGgrRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 14-79 1.73e-24

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: 96.32  E-value: 1.73e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622399   14 LGTRIKIGDN-YGTVRYVGEVSGHMGSWLGIEWDDGlRGKHNGIVDGKRYFQTQtPTGGSFIRPGKV 79
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 443-523 2.14e-24

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: 96.88  E-value: 2.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 443 NLINVSIRHQL--TGETWEKKVPRMITVQTLQGLVMKRFRLSGDVPQLCYVDALHPDLVVPLDNNAKTLDFYSVQEHDTV 520
Cdd:cd17044    1 SLITLTLVCPAapEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 442622399 521 LVQ 523
Cdd:cd17044   81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
131-376 3.50e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 131 SKFEQLEEVSVDQTPVNAAGY-LKELTHLTTLNVSHTLIwnWEIVASIAqQLPSLTNLNLSSNRL-VLP----------- 197
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQL--TDLPEPLG-NLTNLKSLDLSNNQLtDLPeelgnltnlke 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 198 ---TSSQITELEPSF---RQLKRINLRSCGFSDWKDVMHTallWPNILSLGLQENSLGQLAEVDRtkiFKQLHELDLHRT 271
Cdd:COG4886  187 ldlSNNQITDLPEPLgnlTNLEELDLSGNQLTDLPEPLAN---LTNLETLDLSNNQLTDLPELGN---LTNLEELDLSNN 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 272 NIMDFDqvtKLGNLTTLRLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQLNLLHNPIWNEADAFNELDKLPQLKRLSKTP 351
Cdd:COG4886  261 QLTDLP---PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTL 337

                        250       260
                 ....*....|....*....|....*
gi 442622399 352 HLKSNFDEMFSKAVASIASLQFINK 376
Cdd:COG4886  338 TTLALSLSLLALLTLLLLLNLLSLL 362
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 14-76 1.56e-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: 60.47  E-value: 1.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622399  14 LGTRIKIGDNYGTVRYVGEVSGHMGSWLGIEWDDGLrGKHNGIVDGKRYFQTQTPTgGSFIRP 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDPV-GKNDGSVNGVRYFHCKKRH-GIFIRP 66
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 152-246 1.33e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 49.40  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 152 LKELTHLTTLNVSH-------TLIWNWEIVASIAqqlPSLTNLNLSSNRLvlptsSQITELEPsFRQLKRINLRSCGFSD 224
Cdd:cd21340   86 LENLTNLEELHIENqrlppgeKLTFDPRSLAALS---NSLRVLNISGNNI-----DSLEPLAP-LRNLEQLDASNNQISD 156

                         90       100
                 ....*....|....*....|..
gi 442622399 225 WKDVMHTALLWPNILSLGLQEN 246
Cdd:cd21340  157 LEELLDLLSSWPSLRELDLTGN 178
 
Name Accession Description Interval E-value
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 14-79 3.38e-25

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: 98.43  E-value: 3.38e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442622399    14 LGTRIKIGDN--YGTVRYVGEVSGHMGSWLGIEWDDGLRGKHNGIVDGKRYFQTQtPTGGSFIRPGKV 79
Cdd:smart01052   1 VGDRVEVGGGgrRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 14-79 1.73e-24

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: 96.32  E-value: 1.73e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442622399   14 LGTRIKIGDN-YGTVRYVGEVSGHMGSWLGIEWDDGlRGKHNGIVDGKRYFQTQtPTGGSFIRPGKV 79
Cdd:pfam01302   1 VGDRVEVPGGrRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 443-523 2.14e-24

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: 96.88  E-value: 2.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 443 NLINVSIRHQL--TGETWEKKVPRMITVQTLQGLVMKRFRLSGDVPQLCYVDALHPDLVVPLDNNAKTLDFYSVQEHDTV 520
Cdd:cd17044    1 SLITLTLVCPAapEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 442622399 521 LVQ 523
Cdd:cd17044   81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
131-376 3.50e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 131 SKFEQLEEVSVDQTPVNAAGY-LKELTHLTTLNVSHTLIwnWEIVASIAqQLPSLTNLNLSSNRL-VLP----------- 197
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQL--TDLPEPLG-NLTNLKSLDLSNNQLtDLPeelgnltnlke 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 198 ---TSSQITELEPSF---RQLKRINLRSCGFSDWKDVMHTallWPNILSLGLQENSLGQLAEVDRtkiFKQLHELDLHRT 271
Cdd:COG4886  187 ldlSNNQITDLPEPLgnlTNLEELDLSGNQLTDLPEPLAN---LTNLETLDLSNNQLTDLPELGN---LTNLEELDLSNN 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 272 NIMDFDqvtKLGNLTTLRLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQLNLLHNPIWNEADAFNELDKLPQLKRLSKTP 351
Cdd:COG4886  261 QLTDLP---PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTL 337

                        250       260
                 ....*....|....*....|....*
gi 442622399 352 HLKSNFDEMFSKAVASIASLQFINK 376
Cdd:COG4886  338 TTLALSLSLLALLTLLLLLNLLSLL 362
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
152-348 3.36e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.34  E-value: 3.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 152 LKELTHLTTLNVSHTLIwnWEIVASIAqQLPSLTNLNLSSNrlvlptssQITELEPSFRQLKriNLRscgfsdwkdvmht 231
Cdd:COG4886  109 LSNLTNLESLDLSGNQL--TDLPEELA-NLTNLKELDLSNN--------QLTDLPEPLGNLT--NLK------------- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 232 allwpnilSLGLQENSLGQL-AEVDRtkiFKQLHELDLHRTNIMDFDQVtkLGNLTTLRLLNIMENGIEEIKLPdcdsqe 310
Cdd:COG4886  163 --------SLDLSNNQLTDLpEELGN---LTNLKELDLSNNQITDLPEP--LGNLTNLEELDLSGNQLTDLPEP------ 223

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 442622399 311 kLNIFVSLEQLNLLHNPIwneaDAFNELDKLPQLKRLS 348
Cdd:COG4886  224 -LANLTNLETLDLSNNQL----TDLPELGNLTNLEELD 256
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 14-76 1.56e-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: 60.47  E-value: 1.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622399  14 LGTRIKIGDNYGTVRYVGEVSGHMGSWLGIEWDDGLrGKHNGIVDGKRYFQTQTPTgGSFIRP 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDPV-GKNDGSVNGVRYFHCKKRH-GIFIRP 66
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 152-246 1.33e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 49.40  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 152 LKELTHLTTLNVSH-------TLIWNWEIVASIAqqlPSLTNLNLSSNRLvlptsSQITELEPsFRQLKRINLRSCGFSD 224
Cdd:cd21340   86 LENLTNLEELHIENqrlppgeKLTFDPRSLAALS---NSLRVLNISGNNI-----DSLEPLAP-LRNLEQLDASNNQISD 156

                         90       100
                 ....*....|....*....|..
gi 442622399 225 WKDVMHTALLWPNILSLGLQEN 246
Cdd:cd21340  157 LEELLDLLSSWPSLRELDLTGN 178
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
136-348 1.99e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.32  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 136 LEEVSVDQTPVNAAGYLKELTHLTTLNVSHTLIWNWEIVASIAQQLPSLTNLNLSSNRLVLptssqitelepSFRQLKRI 215
Cdd:COG4886   50 TLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS-----------NLTNLESL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 216 NLRSCGFSDWkdvmhtallwpnilslglqENSLGQLaevdrtkifKQLHELDLHRTNIMDFDqvTKLGNLTTLRLLNIME 295
Cdd:COG4886  119 DLSGNQLTDL-------------------PEELANL---------TNLKELDLSNNQLTDLP--EPLGNLTNLKSLDLSN 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442622399 296 NGIEEIKLPdcdsqekLNIFVSLEQLNLLHNPIwneADAFNELDKLPQLKRLS 348
Cdd:COG4886  169 NQLTDLPEE-------LGNLTNLKELDLSNNQI---TDLPEPLGNLTNLEELD 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
131-344 2.21e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.93  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 131 SKFEQLEEVSVDQTPVNAAGY-LKELTHLTTLNVSHTLIwnwEIVASIAQqLPSLTNLNLSSNRLV-LPTSSQITeleps 208
Cdd:COG4886  202 GNLTNLEELDLSGNQLTDLPEpLANLTNLETLDLSNNQL---TDLPELGN-LTNLEELDLSNNQLTdLPPLANLT----- 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 209 frQLKRINLRSCGFSDWKdvmHTALLWPNILSLGLQENSLGQLAEVDRTKIFKQLHELDLHRTNIMDFDQVTKLGNLTTL 288
Cdd:COG4886  273 --NLKTLDLSNNQLTDLK---LKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLL 347

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442622399 289 RLLNIMENGIEEIKLPDCDSQEKLNIFVSLEQLNLLHNPIWNEADAFNELDKLPQL 344
Cdd:COG4886  348 ALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 261-385 5.19e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.47  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 261 KQLHELDLHRTNI-----MDFDQVTKLGNLTTLRLLNIMENGIEEIklpdcdsqEKLNIFVSLEQLNLLHNPIWNEADAF 335
Cdd:cd21340   90 TNLEELHIENQRLppgekLTFDPRSLAALSNSLRVLNISGNNIDSL--------EPLAPLRNLEQLDASNNQISDLEELL 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442622399 336 NELDKLPQLKRLsktpHLKSN----FDEMFSKAVASIASLQFINKAEVTAEQRR 385
Cdd:cd21340  162 DLLSSWPSLREL----DLTGNpvckKPKYRDKIILASKSLEVLDGKEITDTERQ 211
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 148-268 1.65e-05

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: 46.96  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622399 148 AAGYLKELTHLTTLNVSHTLIwNWEIVASIAQQLPSLTNL---NLSSNRLVLPTSSQITELEPSFRQLKRINLRSCGFSD 224
Cdd:cd00116  157 LAKALRANRDLKELNLANNGI-GDAGIRALAEGLKANCNLevlDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442622399 225 WKDV-MHTALLWPNI--LSLGLQENSLGQ-----LAEVDRTKifKQLHELDL 268
Cdd:cd00116  236 AGAAaLASALLSPNIslLTLSLSCNDITDdgakdLAEVLAEK--ESLLELDL 285
 
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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