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Conserved domains on  [gi|568215738|ref|NP_001274731|]
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tubulin-specific chaperone E isoform c [Homo sapiens]

Protein Classification

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; ...
 331-413 1.71e-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: 123.07  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 331 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 410
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568215738 411 LVR 413
Cdd:cd17044   81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
11-232 5.93e-13

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 5.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  11 SQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVltGTL 90
Cdd:COG4886   93 GDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLTDLPEPL--GNL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  91 SVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQLIDENQLylIAHLPRLEQ 168
Cdd:COG4886  159 TNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLTDLPEP--LANLTNLET 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568215738 169 LILSDTGISSLhfpdAGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 232
Cdd:COG4886  233 LDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---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; ...
 331-413 1.71e-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: 123.07  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 331 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 410
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568215738 411 LVR 413
Cdd:cd17044   81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
11-232 5.93e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 5.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  11 SQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVltGTL 90
Cdd:COG4886   93 GDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLTDLPEPL--GNL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  91 SVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQLIDENQLylIAHLPRLEQ 168
Cdd:COG4886  159 TNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLTDLPEP--LANLTNLET 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568215738 169 LILSDTGISSLhfpdAGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 232
Cdd:COG4886  233 LDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 39-266 3.57e-09

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: 56.72  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  39 CPNIRKVDLSKNLLSSWDEVihiaDQLRHLEVLNVSENKLKFPSGsvlTGTLSVLKVLVLNQTGITwaeVLRCVAGCPGL 118
Cdd:cd21340   23 CKNLKVLYLYDNKITKIENL----EFLTNLTHLYLQNNQIEKIEN---LENLVNLKKLYLGGNRIS---VVEGLENLTNL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 119 EELYLESNNIFISER-------PTDVLQTVKLLDLSSNQLIDENQLyliAHLPRLEQLILSDTGISSLHfpdagigckts 191
Cdd:cd21340   93 EELHIENQRLPPGEKltfdprsLAALSNSLRVLNISGNNIDSLEPL---APLRNLEQLDASNNQISDLE----------- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568215738 192 mfpslkylvvndnqisqwSFFNELEKLPSLRALSCLRNPLTKEDKEAETarllIIASIGQLKTLNKCEILPEERR 266
Cdd:cd21340  159 ------------------ELLDLLSSWPSLRELDLTGNPVCKKPKYRDK----IILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
120-279 5.99e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 43.21  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  120 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 199
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  200 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRKAFGNE 279
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGKQ 169
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 39-255 7.53e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  39 CPNIRKV---DLS-KNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITwAEVLRcvAG 114
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPR--GS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 115 CPGLEELYLeSNNIFISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDTGISslhfpdAGIGCKTSM 192
Cdd:PLN00113 139 IPNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568215738 193 FPSLKYLVVNDNQISQwSFFNELEKLPSLRALSCLRNPLTKEdkeaetarllIIASIGQLKTL 255
Cdd:PLN00113 211 MKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLTGP----------IPSSLGNLKNL 262
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 343-412 2.17e-04

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 39.82  E-value: 2.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568215738  343 LDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKkpGREI-ELENDLKSLQFYSVENGDCLLV 412
Cdd:pfam14560  10 TKAVSSERRFDKSLTIEELKEKLELITGTPPSSMRLQLYDDD--DNLVaKLDDDDALLGSYGVRDGMRIHV 78
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 333-408 1.54e-03

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: 36.85  E-value: 1.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568215738   333 LTLKIKyphQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYEspkkpGREIElenDLKSLQFYSVENGD 408
Cdd:smart00213   1 IELTVK---TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----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; ...
 331-413 1.71e-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: 123.07  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 331 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 410
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568215738 411 LVR 413
Cdd:cd17044   81 LVR 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
11-232 5.93e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 5.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  11 SQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVltGTL 90
Cdd:COG4886   93 GDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLTDLPEPL--GNL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  91 SVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQLIDENQLylIAHLPRLEQ 168
Cdd:COG4886  159 TNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLTDLPEP--LANLTNLET 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568215738 169 LILSDTGISSLhfpdAGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 232
Cdd:COG4886  233 LDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
11-246 1.58e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.81  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  11 SQLSKLQEVSLRNCAVSCAGEKggvAEACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLK-FPSGSvltGT 89
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEE---LANLTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTdLPEEL---GN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  90 LSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQLIDenqLYLIAHLPRLE 167
Cdd:COG4886  181 LTNLKELDLSNNQIT--DLPEPLGNLTNLEELDLSGNQL--TDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNLE 253

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568215738 168 QLILSDTGISSLHfpdagigcKTSMFPSLKYLVVNDNQISQWSffneLEKLPSLRALSCLRNPLTKEDKEAETARLLII 246
Cdd:COG4886  254 ELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQLTDLK----LKELELLLGLNSLLLLLLLLNLLELLILLLLL 320
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
37-243 9.27e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.11  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  37 EACPNIRKVDLSKNLLSSwdevihiadQLRHLEVLNVSENKLKFPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCP 116
Cdd:COG4886   93 GDLTNLTELDLSGNEELS---------NLTNLESLDLSGNQLTDLPEEL--ANLTNLKELDLSNNQLT--DLPEPLGNLT 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 117 GLEELYLESNNIfiSERPTDVLQTVKL--LDLSSNQLIDENQLylIAHLPRLEQLILSDTGISSLhfPDAGIGCKtsmfp 194
Cdd:COG4886  160 NLKSLDLSNNQL--TDLPEELGNLTNLkeLDLSNNQITDLPEP--LGNLTNLEELDLSGNQLTDL--PEPLANLT----- 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568215738 195 SLKYLVVNDNQISQWSffnELEKLPSLRALSCLRNPLTKEDKEAETARL 243
Cdd:COG4886  229 NLETLDLSNNQLTDLP---ELGNLTNLEELDLSNNQLTDLPPLANLTNL 274
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 39-266 3.57e-09

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: 56.72  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  39 CPNIRKVDLSKNLLSSWDEVihiaDQLRHLEVLNVSENKLKFPSGsvlTGTLSVLKVLVLNQTGITwaeVLRCVAGCPGL 118
Cdd:cd21340   23 CKNLKVLYLYDNKITKIENL----EFLTNLTHLYLQNNQIEKIEN---LENLVNLKKLYLGGNRIS---VVEGLENLTNL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 119 EELYLESNNIFISER-------PTDVLQTVKLLDLSSNQLIDENQLyliAHLPRLEQLILSDTGISSLHfpdagigckts 191
Cdd:cd21340   93 EELHIENQRLPPGEKltfdprsLAALSNSLRVLNISGNNIDSLEPL---APLRNLEQLDASNNQISDLE----------- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568215738 192 mfpslkylvvndnqisqwSFFNELEKLPSLRALSCLRNPLTKEDKEAETarllIIASIGQLKTLNKCEILPEERR 266
Cdd:cd21340  159 ------------------ELLDLLSSWPSLRELDLTGNPVCKKPKYRDK----IILASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
5-230 2.03e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.71  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738   5 ELCFSCSQLSKLQEVSLRNCAVSCAGEkggVAEACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLKFPSGS 84
Cdd:COG4886  150 DLPEPLGNLTNLKSLDLSNNQLTDLPE---ELGNLTNLKELDLSNNQITDLPEPL---GNLTNLEELDLSGNQLTDLPEP 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  85 VltGTLSVLKVLVLNQTGITwaeVLRCVAGCPGLEELYLESNNIfISERPTDVLQTVKLLDLSSNQLIDENqlylIAHLP 164
Cdd:COG4886  224 L--ANLTNLETLDLSNNQLT---DLPELGNLTNLEELDLSNNQL-TDLPPLANLTNLKTLDLSNNQLTDLK----LKELE 293

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568215738 165 RLEQLILSDTGISSLHFPDAGIGCKTSMFPSLKYLVVNDNQISQWSFFNELEKLPSLRALSCLRNP 230
Cdd:COG4886  294 LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLL 359
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 4-154 2.99e-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: 45.81  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738   4 CELCFSCSQLSKLQEVSLRNCAVSCAGEK---GGVAEACPNIRKVDLSKNLLSSwDEVIHIADQLRH---LEVLNVSENK 77
Cdd:cd00116   98 CGVLESLLRSSSLQELKLNNNGLGDRGLRllaKGLKDLPPALEKLVLGRNRLEG-ASCEALAKALRAnrdLKELNLANNG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  78 LKFPSGSVLTGTL---SVLKVLVLNQTGITWAEVLR---CVAGCPGLEELYLESNNI------FISERPTDVLQTVKLLD 145
Cdd:cd00116  177 IGDAGIRALAEGLkanCNLEVLDLNNNGLTDEGASAlaeTLASLKSLEVLNLGDNNLtdagaaALASALLSPNISLLTLS 256


                 ....*....
gi 568215738 146 LSSNQLIDE 154
Cdd:cd00116  257 LSCNDITDD 265
LRR_9 pfam14580
Leucine-rich repeat;
120-279 5.99e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 43.21  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  120 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 199
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  200 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRKAFGNE 279
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGKQ 169
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 335-413 7.04e-05

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: 40.66  E-value: 7.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568215738 335 LKIKYPhqlDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYespkkpgREIELENDlKSLQFYSVENGDCLLVR 413
Cdd:cd17039    1 ITVKTL---DGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 39-255 7.53e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.22  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  39 CPNIRKV---DLS-KNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITwAEVLRcvAG 114
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPR--GS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 115 CPGLEELYLeSNNIFISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDTGISslhfpdAGIGCKTSM 192
Cdd:PLN00113 139 IPNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568215738 193 FPSLKYLVVNDNQISQwSFFNELEKLPSLRALSCLRNPLTKEdkeaetarllIIASIGQLKTL 255
Cdd:PLN00113 211 MKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLTGP----------IPSSLGNLKNL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
65-256 1.57e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  65 LRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITWAEVLRCVAGCPGLEELYLESNNIFISERPTDVLQTVKLL 144
Cdd:COG4886   14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738 145 DLSSNQLIDENQLYLIAHLPRLEQLILSDTGISSLhfPDAgigckTSMFPSLKYLVVNDNQISqwSFFNELEKLPSLRAL 224
Cdd:COG4886   94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDL--PEE-----LANLTNLKELDLSNNQLT--DLPEPLGNLTNLKSL 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568215738 225 SCLRNPLTKEDKEaetarlliIASIGQLKTLN 256
Cdd:COG4886  165 DLSNNQLTDLPEE--------LGNLTNLKELD 188
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 343-412 2.17e-04

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 39.82  E-value: 2.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568215738  343 LDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKkpGREI-ELENDLKSLQFYSVENGDCLLV 412
Cdd:pfam14560  10 TKAVSSERRFDKSLTIEELKEKLELITGTPPSSMRLQLYDDD--DNLVaKLDDDDALLGSYGVRDGMRIHV 78
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 41-176 1.48e-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: 40.54  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  41 NIRKVDLSKNLLSSwDEVIHIADQLR---HLEVLNVSENKLKFPSGSVLTGTL---SVLKVLVLNQTGITWAEVLRCVAG 114
Cdd:COG5238  265 TVETLYLSGNQIGA-EGAIALAKALQgntTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIGAQGAIALAKA 343

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568215738 115 C---PGLEELYLESNNIfiSERPTDVL-------QTVKLLDLSSNQLIDENQLYLIAHL--PRLEQLILSDTGI 176
Cdd:COG5238  344 LqenTTLHSLDLSDNQI--GDEGAIALakylegnTTLRELNLGKNNIGKQGAEALIDALqtNRLHTLILDGNLI 415
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 333-408 1.54e-03

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: 36.85  E-value: 1.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568215738   333 LTLKIKyphQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYEspkkpGREIElenDLKSLQFYSVENGD 408
Cdd:smart00213   1 IELTVK---TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 30-169 2.13e-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: 40.16  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  30 GEKG--GVAEA---CPNIRKVDLSKNLLSswDE-VIHIADQLRH---LEVLNVSENKLKfPSGSVLTG-------TLSVL 93
Cdd:COG5238  277 GAEGaiALAKAlqgNTTLTSLDLSVNRIG--DEgAIALAEGLQGnktLHTLNLAYNGIG-AQGAIALAkalqentTLHSL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215738  94 KvLVLNQTGITWAEVL-RCVAGCPGLEELYLESNNIFISERPT--DVLQTVKL--LDLSSNQLIDENQLYLIAHLPRLEQ 168
Cdd:COG5238  354 D-LSDNQIGDEGAIALaKYLEGNTTLRELNLGKNNIGKQGAEAliDALQTNRLhtLILDGNLIGAEAQQRLEQLLERIKS 432


                 .
gi 568215738 169 L 169
Cdd:COG5238  433 V 433
LRR_8 pfam13855
Leucine rich repeat;
116-176 4.42e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.19  E-value: 4.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568215738  116 PGLEELYLESNNI-FISERPTDVLQTVKLLDLSSNQL--IDENQLyliAHLPRLEQLILSDTGI 176
Cdd:pfam13855   1 PNLRSLDLSNNRLtSLDDGAFKGLSNLKVLDLSNNLLttLSPGAF---SGLPSLRYLDLSGNRL 61
 
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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