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Conserved domains on  [gi|966923993|ref|XP_014982046|]
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tubulin-specific chaperone E isoform X1 [Macaca mulatta]

Protein Classification

CAP_GLY and Ubl_TBCE domain-containing protein( domain architecture ID 13651372)

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 pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
10-75 2.51e-25

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: 98.63  E-value: 2.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966923993   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFVRPNKV 75
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
444-497 5.87e-16

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: 73.00  E-value: 5.87e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966923993 444 QLLTLKIKYPDQLDQKVLEKQLPGSMTIQKVKGWLSRLLKVPVSDLLLSYESPK 497
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSE 54
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
117-345 4.11e-15

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.28  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 117 DSLMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRRVDLSKNLLSSWDEVIHiadQLRHLEVLNLSENKLK-FPS 195
Cdd:COG4886   86 LLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLTdLPE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 196 gsALtGTFSALKVLVLNQTGITwaEVLRCAAWCPGLEELYLESNNIviSERPTDV--LQTVKLLDLSSNQL--IDENqly 271
Cdd:COG4886  154 --PL-GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP--- 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966923993 272 lIAHLPRLEQLILSDIGISSIhfpdAGIGCktsmFPSLQYLVVNDNQISQwsfFNELDKLPSLRALSCLRNPLT 345
Cdd:COG4886  224 -LANLTNLETLDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
10-75 2.51e-25

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: 98.63  E-value: 2.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966923993   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFVRPNKV 75
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
10-75 7.62e-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: 97.66  E-value: 7.62e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966923993    10 IGRRVEV--NGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRhPTGGSFVRPNKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
444-497 5.87e-16

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: 73.00  E-value: 5.87e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966923993 444 QLLTLKIKYPDQLDQKVLEKQLPGSMTIQKVKGWLSRLLKVPVSDLLLSYESPK 497
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSE 54
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
117-345 4.11e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.28  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 117 DSLMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRRVDLSKNLLSSWDEVIHiadQLRHLEVLNLSENKLK-FPS 195
Cdd:COG4886   86 LLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLTdLPE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 196 gsALtGTFSALKVLVLNQTGITwaEVLRCAAWCPGLEELYLESNNIviSERPTDV--LQTVKLLDLSSNQL--IDENqly 271
Cdd:COG4886  154 --PL-GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP--- 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966923993 272 lIAHLPRLEQLILSDIGISSIhfpdAGIGCktsmFPSLQYLVVNDNQISQwsfFNELDKLPSLRALSCLRNPLT 345
Cdd:COG4886  224 -LANLTNLETLDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
172-380 1.30e-10

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: 61.34  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 172 IHIADQLRHLEVLNLSENKLkfpsgSALTG--TFSALKVLVL--NQtgITWAEVLRCaawCPGLEELYLESNNI-VIS-- 244
Cdd:cd21340   17 IDNLSLCKNLKVLYLYDNKI-----TKIENleFLTNLTHLYLqnNQ--IEKIENLEN---LVNLKKLYLGGNRIsVVEgl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 245 ERPTDvLQTvklLDLSSNQLIDENQLY-----LIAHLPRLEQLILSDIGISSIhfpdAGIGCktsmFPSLQYLVVNDNQI 319
Cdd:cd21340   87 ENLTN-LEE---LHIENQRLPPGEKLTfdprsLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQI 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966923993 320 SQWS-FFNELDKLPSLRALSCLRNPLTKEDKEanmtRQLIIASIGQLKTLNKCEILPKERRT 380
Cdd:cd21340  155 SDLEeLLDLLSSWPSLRELDLTGNPVCKKPKY----RDKIILASKSLEVLDGKEITDTERQF 212
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
10-76 5.81e-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: 58.54  E-value: 5.81e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966923993  10 IGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTgGSFVRPNKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
LRR_9 pfam14580
Leucine-rich repeat;
233-396 5.15e-06

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 47.07  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993  233 ELYLESNNIVISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDIGISSIhfpDAGIGcktSMFPSLQYL 312
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993  313 VVNDNQISQWSFFNELDKLPSLRALSCLRNPLTKEDKeanmTRQLIIASIGQLKTLNKCEILPKERRTAELDYRkafGNE 392
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPH----YRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166

                  ....
gi 966923993  393 WKQA 396
Cdd:pfam14580 167 GKQL 170
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
152-368 7.24e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.08  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 152 CPNIRRV---DLS-KNLLSSWDEVIHiadQLRHLEVLNLSENKLKFPSGSALTGTFSALKVLVLNQTGITwAEVLRCAAw 227
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPRGSI- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 228 cPGLEELYLeSNNIVISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDIGISsihfpdAGIGCKTSM 305
Cdd:PLN00113 140 -PNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923993 306 FPSLQYLVVNDNQISQwSFFNELDKLPSLRALSCLRNPLTKEdkeanmtrqlIIASIGQLKTL 368
Cdd:PLN00113 211 MKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLTGP----------IPSSLGNLKNL 262
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
10-75 2.51e-25

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: 98.63  E-value: 2.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966923993   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFVRPNKV 75
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
10-75 7.62e-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: 97.66  E-value: 7.62e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966923993    10 IGRRVEV--NGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRhPTGGSFVRPNKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
444-497 5.87e-16

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: 73.00  E-value: 5.87e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966923993 444 QLLTLKIKYPDQLDQKVLEKQLPGSMTIQKVKGWLSRLLKVPVSDLLLSYESPK 497
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSE 54
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
117-345 4.11e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.28  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 117 DSLMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRRVDLSKNLLSSWDEVIHiadQLRHLEVLNLSENKLK-FPS 195
Cdd:COG4886   86 LLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLTdLPE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 196 gsALtGTFSALKVLVLNQTGITwaEVLRCAAWCPGLEELYLESNNIviSERPTDV--LQTVKLLDLSSNQL--IDENqly 271
Cdd:COG4886  154 --PL-GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP--- 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966923993 272 lIAHLPRLEQLILSDIGISSIhfpdAGIGCktsmFPSLQYLVVNDNQISQwsfFNELDKLPSLRALSCLRNPLT 345
Cdd:COG4886  224 -LANLTNLETLDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
172-380 1.30e-10

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: 61.34  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 172 IHIADQLRHLEVLNLSENKLkfpsgSALTG--TFSALKVLVL--NQtgITWAEVLRCaawCPGLEELYLESNNI-VIS-- 244
Cdd:cd21340   17 IDNLSLCKNLKVLYLYDNKI-----TKIENleFLTNLTHLYLqnNQ--IEKIENLEN---LVNLKKLYLGGNRIsVVEgl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 245 ERPTDvLQTvklLDLSSNQLIDENQLY-----LIAHLPRLEQLILSDIGISSIhfpdAGIGCktsmFPSLQYLVVNDNQI 319
Cdd:cd21340   87 ENLTN-LEE---LHIENQRLPPGEKLTfdprsLAALSNSLRVLNISGNNIDSL----EPLAP----LRNLEQLDASNNQI 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966923993 320 SQWS-FFNELDKLPSLRALSCLRNPLTKEDKEanmtRQLIIASIGQLKTLNKCEILPKERRT 380
Cdd:cd21340  155 SDLEeLLDLLSSWPSLRELDLTGNPVCKKPKY----RDKIILASKSLEVLDGKEITDTERQF 212
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
116-343 2.06e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 116 FDSLMKQQSQLSKLQEVSLRNCAVSCAGEkggVAEACPNIRRVDLSKNLLSSWDEVIhiaDQLRHLEVLNLSENKLKFPS 195
Cdd:COG4886  148 LTDLPEPLGNLTNLKSLDLSNNQLTDLPE---ELGNLTNLKELDLSNNQITDLPEPL---GNLTNLEELDLSGNQLTDLP 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 196 GSalTGTFSALKVLVLNQTGITWAEVLRCaawCPGLEELYLESNNIvISERPTDVLQTVKLLDLSSNQLIDENqlylIAH 275
Cdd:COG4886  222 EP--LANLTNLETLDLSNNQLTDLPELGN---LTNLEELDLSNNQL-TDLPPLANLTNLKTLDLSNNQLTDLK----LKE 291
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966923993 276 LPRLEQLILSDIGISSIHFPDAGIGCKTSMFPSLQYLVVNDNQISQWSFFNELDKLPSLRALSCLRNP 343
Cdd:COG4886  292 LELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLL 359
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
10-76 5.81e-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: 58.54  E-value: 5.81e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966923993  10 IGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTgGSFVRPNKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
124-267 3.45e-06

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: 48.89  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 124 SQLSKLQEVSLRNCAVSCAGEK---GGVAEACPNIRRVDLSKNLLSSwDEVIHIADQLRH---LEVLNLSENKLKfPSGS 197
Cdd:cd00116  105 LRSSSLQELKLNNNGLGDRGLRllaKGLKDLPPALEKLVLGRNRLEG-ASCEALAKALRAnrdLKELNLANNGIG-DAGI 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 198 ALTG----TFSALKVLVLNQTGITWAEvlrCAAWC------PGLEELYLESNNI------VISERPTDVLQTVKLLDLSS 261
Cdd:cd00116  183 RALAeglkANCNLEVLDLNNNGLTDEG---ASALAetlaslKSLEVLNLGDNNLtdagaaALASALLSPNISLLTLSLSC 259

                 ....*.
gi 966923993 262 NQLIDE 267
Cdd:cd00116  260 NDITDD 265
LRR_9 pfam14580
Leucine-rich repeat;
233-396 5.15e-06

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 47.07  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993  233 ELYLESNNIVISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDIGISSIhfpDAGIGcktSMFPSLQYL 312
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993  313 VVNDNQISQWSFFNELDKLPSLRALSCLRNPLTKEDKeanmTRQLIIASIGQLKTLNKCEILPKERRTAELDYRkafGNE 392
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPH----YRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166

                  ....
gi 966923993  393 WKQA 396
Cdd:pfam14580 167 GKQL 170
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
152-368 7.24e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.08  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 152 CPNIRRV---DLS-KNLLSSWDEVIHiadQLRHLEVLNLSENKLKFPSGSALTGTFSALKVLVLNQTGITwAEVLRCAAw 227
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPRGSI- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 228 cPGLEELYLeSNNIVISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDIGISsihfpdAGIGCKTSM 305
Cdd:PLN00113 140 -PNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923993 306 FPSLQYLVVNDNQISQwSFFNELDKLPSLRALSCLRNPLTKEdkeanmtrqlIIASIGQLKTL 368
Cdd:PLN00113 211 MKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLTGP----------IPSSLGNLKNL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
178-370 2.02e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 178 LRHLEVLNLSENKLKFPSGSALTGTFSALKVLVLNQTGITWAEVLRCAAWCPGLEELYLESNNIVISERPTDVLQTVKLL 257
Cdd:COG4886   14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 258 DLSSNQLIDENQLYLIAHLPRLEQLILSDIGISSIhfPDAgigckTSMFPSLQYLVVNDNQISqwSFFNELDKLPSLRAL 337
Cdd:COG4886   94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDL--PEE-----LANLTNLKELDLSNNQLT--DLPEPLGNLTNLKSL 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 966923993 338 SCLRNPLTKEDKE-ANMT--RQLII---------ASIGQLKTLNK 370
Cdd:COG4886  165 DLSNNQLTDLPEElGNLTnlKELDLsnnqitdlpEPLGNLTNLEE 209
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
102-289 3.31e-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: 46.32  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 102 QIVTLGNKPVETVGFDSLMKQQSQLSKLQEVSLRNCAVscaGEKG--GVAEA---CPNIRRVDLSKNLLSSwDEVIHIAD 176
Cdd:COG5238  183 ETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPI---GDEGaeILAEAlkgNKSLTTLDLSNNQIGD-EGVIALAE 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 177 QLR-------------------------------HLEVLNLSENKLKFPSGSALTGTF---SALKVLVLNQTGITWAEVL 222
Cdd:COG5238  259 ALKnnttvetlylsgnqigaegaialakalqgntTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIGAQGAI 338
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966923993 223 RCAA---WCPGLEELYLESNNIviSERPTDVL-------QTVKLLDLSSNQLIDENQLYLIAHL--PRLEQLILSDIGI 289
Cdd:COG5238  339 ALAKalqENTTLHSLDLSDNQI--GDEGAIALakylegnTTLRELNLGKNNIGKQGAEALIDALqtNRLHTLILDGNLI 415
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
126-350 8.94e-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: 41.57  E-value: 8.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 126 LSKLQEVSLRNCAVSCAGEkgGVAEAC---PNIRRVDLSKNLLSSwDEVIHIADQLRH----LEVLNLSENKLKFPSGSA 198
Cdd:cd00116   80 GCGLQELDLSDNALGPDGC--GVLESLlrsSSLQELKLNNNGLGD-RGLRLLAKGLKDlppaLEKLVLGRNRLEGASCEA 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 199 LTGTFSA---LKVLVLNQTGITWAEVlrcAAWCPGLEElylesnniviserptdvLQTVKLLDLSSNQLIDENQLYL--- 272
Cdd:cd00116  157 LAKALRAnrdLKELNLANNGIGDAGI---RALAEGLKA-----------------NCNLEVLDLNNNGLTDEGASALaet 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 273 IAHLPRLEQLILSDIGISsihfpDAGIGCKTSMFP----SLQYLVVNDNQISQWSFFNE---LDKLPSLRALSCLRNPLT 345
Cdd:cd00116  217 LASLKSLEVLNLGDNNLT-----DAGAAALASALLspniSLLTLSLSCNDITDDGAKDLaevLAEKESLLELDLRGNKFG 291

                 ....*
gi 966923993 346 KEDKE 350
Cdd:cd00116  292 EEGAQ 296
LRR_8 pfam13855
Leucine rich repeat;
229-286 1.66e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966923993  229 PGLEELYLESNNI-VISERPTDVLQTVKLLDLSSNQL--IDENQLyliAHLPRLEQLILSD 286
Cdd:pfam13855   1 PNLRSLDLSNNRLtSLDDGAFKGLSNLKVLDLSNNLLttLSPGAF---SGLPSLRYLDLSG 58
LRR_8 pfam13855
Leucine rich repeat;
153-216 1.92e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 1.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966923993  153 PNIRRVDLSKNLLSswdeviHIADQ----LRHLEVLNLSENKLKFPSGSALTGtFSALKVLVLNQTGI 216
Cdd:pfam13855   1 PNLRSLDLSNNRLT------SLDDGafkgLSNLKVLDLSNNLLTTLSPGAFSG-LPSLRYLDLSGNRL 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
143-282 7.93e-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: 38.62  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 143 GEKG--GVAEA---CPNIRRVDLSKNLLSswDE-VIHIADQLRH---LEVLNLSENKLkfpSGSALTGTFSALKV----- 208
Cdd:COG5238  277 GAEGaiALAKAlqgNTTLTSLDLSVNRIG--DEgAIALAEGLQGnktLHTLNLAYNGI---GAQGAIALAKALQEnttlh 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923993 209 ---LVLNQTGITWAEVLRCA-AWCPGLEELYLESNNIVISERPT--DVLQTVKL--LDLSSNQLIDENQLYLIAHLPRLE 280
Cdd:COG5238  352 sldLSDNQIGDEGAIALAKYlEGNTTLRELNLGKNNIGKQGAEAliDALQTNRLhtLILDGNLIGAEAQQRLEQLLERIK 431

                 ..
gi 966923993 281 QL 282
Cdd:COG5238  432 SV 433
Ubl_IQUB cd17061
ubiquitin-like (Ubl) domain found in IQ and ubiquitin-like domain-containing protein (IQUB) ...
470-520 8.16e-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: 35.32  E-value: 8.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 966923993 470 TIQKVKGWLSRLLKVPVSDLLLSYESPKVscpgKNKVKL-----RPHDDIKLSLDS 520
Cdd:cd17061   25 TIGELKEHFSSELKIPPDVLQIMFDGKLV----EDNTTLvdlgvRPNGTIQLEMSS 76
 
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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