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Conserved domains on  [gi|568215736|ref|NP_001274730|]
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tubulin-specific chaperone E isoform b [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; ...
 495-577 9.49e-35

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: 125.77  E-value: 9.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 495 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 574
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568215736 575 LVR 577
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 1.30e-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: 97.09  E-value: 1.30e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568215736   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 75
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
Ribosomal_S21e super family cl03140
Ribosomal protein S21e;
234-272 5.73e-13

Ribosomal protein S21e;


The actual alignment was detected with superfamily member pfam01249:

Pssm-ID: 460133  Cd Length: 79  Bit Score: 64.47  E-value: 5.73e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568215736  234 MQKDASKFVDLCVLQKCSTSNCIISAKDHTSMRMNVAKV 272
Cdd:pfam01249   1 MQNDAGELVDLYIPRKCSATNRLITAKDHASVQINVAEV 39
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-396 7.29e-11

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.18  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 193 -FPsgSVLtGTLSVLKVLVLNQTGITwaeahaqcggsrhgldmqkdaskfvdlcvlqkcstsnciisakdhtsmrmNVAK 271
Cdd:COG4886  150 dLP--EPL-GNLTNLKSLDLSNNQLT--------------------------------------------------DLPE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 272 VLrcvAGCPGLEELYLESNNifISERPTDV--LQTVKLLDLSSNQL--IDENqlylIAHLPRLEQLILSDTGISSLhfpd 347
Cdd:COG4886  177 EL---GNLTNLKELDLSNNQ--ITDLPEPLgnLTNLEELDLSGNQLtdLPEP----LANLTNLETLDLSNNQLTDL---- 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568215736 348 AGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 396
Cdd:COG4886  244 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; ...
 495-577 9.49e-35

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: 125.77  E-value: 9.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 495 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 574
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568215736 575 LVR 577
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 1.30e-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: 97.09  E-value: 1.30e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568215736   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 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 3.42e-24

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: 95.73  E-value: 3.42e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568215736    10 IGRRVEV--NGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Ribosomal_S21e pfam01249
Ribosomal protein S21e;
234-272 5.73e-13

Ribosomal protein S21e;


Pssm-ID: 460133  Cd Length: 79  Bit Score: 64.47  E-value: 5.73e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568215736  234 MQKDASKFVDLCVLQKCSTSNCIISAKDHTSMRMNVAKV 272
Cdd:pfam01249   1 MQNDAGELVDLYIPRKCSATNRLITAKDHASVQINVAEV 39
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-396 7.29e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.18  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 193 -FPsgSVLtGTLSVLKVLVLNQTGITwaeahaqcggsrhgldmqkdaskfvdlcvlqkcstsnciisakdhtsmrmNVAK 271
Cdd:COG4886  150 dLP--EPL-GNLTNLKSLDLSNNQLT--------------------------------------------------DLPE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 272 VLrcvAGCPGLEELYLESNNifISERPTDV--LQTVKLLDLSSNQL--IDENqlylIAHLPRLEQLILSDTGISSLhfpd 347
Cdd:COG4886  177 EL---GNLTNLKELDLSNNQ--ITDLPEPLgnLTNLEELDLSGNQLtdLPEP----LANLTNLETLDLSNNQLTDL---- 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568215736 348 AGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 396
Cdd:COG4886  244 PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 278-430 3.01e-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: 57.49  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 278 GCPGLEELYLESNNIF-IS--ERPTDvLQTvklLDLSSNQLIDENQLY-----LIAHLPRLEQLILSDTGISSLhfpdAG 349
Cdd:cd21340   66 NLVNLKKLYLGGNRISvVEglENLTN-LEE---LHIENQRLPPGEKLTfdprsLAALSNSLRVLNISGNNIDSL----EP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 350 IGCktsmFPSLKYLVVNDNQISQWS-FFNELEKLPSLRALSCLRNPLTKEDKEAETarllIIASIGQLKTLNKCEILPEE 428
Cdd:cd21340  138 LAP----LRNLEQLDASNNQISDLEeLLDLLSSWPSLRELDLTGNPVCKKPKYRDK----IILASKSLEVLDGKEITDTE 209


                 ..
gi 568215736 429 RR 430
Cdd:cd21340  210 RQ 211
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 6.75e-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: 6.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568215736  10 IGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTgGSFIRPNKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
LRR_9 pfam14580
Leucine-rich repeat;
284-447 2.58e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 45.14  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736  284 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 363
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736  364 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRkafGNE 443
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166


                  ....
gi 568215736  444 WKQA 447
Cdd:pfam14580 167 GKQL 170
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 507-576 3.32e-04

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


Pssm-ID: 405277  Cd Length: 83  Bit Score: 39.43  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568215736  507 LDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKkpGREI-ELENDLKSLQFYSVENGDCLLV 576
Cdd:pfam14560  10 TKAVSSERRFDKSLTIEELKEKLELITGTPPSSMRLQLYDDD--DNLVaKLDDDDALLGSYGVRDGMRIHV 78
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 497-572 1.47e-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: 37.62  E-value: 1.47e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568215736   497 LTLKIKyphQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYEspkkpGREIElenDLKSLQFYSVENGD 572
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; ...
 495-577 9.49e-35

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: 125.77  E-value: 9.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 495 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 574
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 568215736 575 LVR 577
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 1.30e-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: 97.09  E-value: 1.30e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568215736   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 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 3.42e-24

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: 95.73  E-value: 3.42e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568215736    10 IGRRVEV--NGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Ribosomal_S21e pfam01249
Ribosomal protein S21e;
234-272 5.73e-13

Ribosomal protein S21e;


Pssm-ID: 460133  Cd Length: 79  Bit Score: 64.47  E-value: 5.73e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568215736  234 MQKDASKFVDLCVLQKCSTSNCIISAKDHTSMRMNVAKV 272
Cdd:pfam01249   1 MQNDAGELVDLYIPRKCSATNRLITAKDHASVQINVAEV 39
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-396 7.29e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.18  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 193 -FPsgSVLtGTLSVLKVLVLNQTGITwaeahaqcggsrhgldmqkdaskfvdlcvlqkcstsnciisakdhtsmrmNVAK 271
Cdd:COG4886  150 dLP--EPL-GNLTNLKSLDLSNNQLT--------------------------------------------------DLPE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 272 VLrcvAGCPGLEELYLESNNifISERPTDV--LQTVKLLDLSSNQL--IDENqlylIAHLPRLEQLILSDTGISSLhfpd 347
Cdd:COG4886  177 EL---GNLTNLKELDLSNNQ--ITDLPEPLgnLTNLEELDLSGNQLtdLPEP----LANLTNLETLDLSNNQLTDL---- 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568215736 348 AGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 396
Cdd:COG4886  244 PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
276-419 1.07e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.80  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 276 VAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDENqlylIAHLPRLEQLILSDTGISSLHFPdagIG 351
Cdd:COG4886  132 LANLTNLKELDLSNNQL--TDLPEPLgnLTNLKSLDLSNNQLtdLPEE----LGNLTNLKELDLSNNQITDLPEP---LG 202

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568215736 352 CktsmFPSLKYLVVNDNQISqwSFFNELEKLPSLRALSCLRNPLTKedkeaetarlliIASIGQLKTL 419
Cdd:COG4886  203 N----LTNLEELDLSGNQLT--DLPEPLANLTNLETLDLSNNQLTD------------LPELGNLTNL 252
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
276-420 1.39e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.41  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 276 VAGCPGLEELYLESNNifISERPTDV--LQTVKLLDLSSNQL--IDENqlylIAHLPRLEQLILSDTGISSLhfPDAGIG 351
Cdd:COG4886  109 LSNLTNLESLDLSGNQ--LTDLPEELanLTNLKELDLSNNQLtdLPEP----LGNLTNLKSLDLSNNQLTDL--PEELGN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568215736 352 CktsmfPSLKYLVVNDNQISQWSffNELEKLPSLRALSCLRNPLTKEDKEaetarlliIASIGQLKTLN 420
Cdd:COG4886  181 L-----TNLKELDLSNNQITDLP--EPLGNLTNLEELDLSGNQLTDLPEP--------LANLTNLETLD 234
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 278-430 3.01e-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: 57.49  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 278 GCPGLEELYLESNNIF-IS--ERPTDvLQTvklLDLSSNQLIDENQLY-----LIAHLPRLEQLILSDTGISSLhfpdAG 349
Cdd:cd21340   66 NLVNLKKLYLGGNRISvVEglENLTN-LEE---LHIENQRLPPGEKLTfdprsLAALSNSLRVLNISGNNIDSL----EP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 350 IGCktsmFPSLKYLVVNDNQISQWS-FFNELEKLPSLRALSCLRNPLTKEDKEAETarllIIASIGQLKTLNKCEILPEE 428
Cdd:cd21340  138 LAP----LRNLEQLDASNNQISDLEeLLDLLSSWPSLRELDLTGNPVCKKPKYRDK----IILASKSLEVLDGKEITDTE 209


                 ..
gi 568215736 429 RR 430
Cdd:cd21340  210 RQ 211
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 6.75e-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: 6.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568215736  10 IGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTgGSFIRPNKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-410 1.22e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.09  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 124 SQLSKLQEVSLRNCAVSCAGEKGGvaeACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLkfpsgSVLTGTL 203
Cdd:COG4886  133 ANLTNLKELDLSNNQLTDLPEPLG---NLTNLKSLDLSNNQLTDLPEEL---GNLTNLKELDLSNNQI-----TDLPEPL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 204 SvlkvlvlnqtgitwaeahaqcggsrhgldmqkdaskfvdlcvlqkcstsnciisakdhtsmrmnvakvlrcvaGCPGLE 283
Cdd:COG4886  202 G-------------------------------------------------------------------------NLTNLE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 284 ELYLESNNifISERPTDV--LQTVKLLDLSSNQLIDenqLYLIAHLPRLEQLILSDTGISSLhfPDAGIgcktsmFPSLK 361
Cdd:COG4886  209 ELDLSGNQ--LTDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNLEELDLSNNQLTDL--PPLAN------LTNLK 275

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568215736 362 YLVVNDNQISQWSffneLEKLPSLRALSCLRNPLTKEDKEAETARLLII 410
Cdd:COG4886  276 TLDLSNNQLTDLK----LKELELLLGLNSLLLLLLLLNLLELLILLLLL 320
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 124-335 4.52e-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: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 124 SQLSKLQEVSLRNCAVSCAGEK---GGVAEACPNIRKVDLSKNLLSSwDEVIHIADQLRH---LEVLNVSENKLKFPSGS 197
Cdd:cd00116  105 LRSSSLQELKLNNNGLGDRGLRllaKGLKDLPPALEKLVLGRNRLEG-ASCEALAKALRAnrdLKELNLANNGIGDAGIR 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 198 VLTGTL---SVLKVLVLNQTGITWAEAHAQCGGsrhgldmqkdaskFVDLCVLQKCSTSNCIISAKD----HTSMRMNVA 270
Cdd:cd00116  184 ALAEGLkanCNLEVLDLNNNGLTDEGASALAET-------------LASLKSLEVLNLGDNNLTDAGaaalASALLSPNI 250

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568215736 271 KVLRCVAGCPGLEELYLESNNIFISERPtdvlqTVKLLDLSSNQLIDENQ--LYLIAHLPRLEQLIL 335
Cdd:cd00116  251 SLLTLSLSCNDITDDGAKDLAEVLAEKE-----SLLELDLRGNKFGEEGAqlLAESLLEPGNELESL 312
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
302-428 6.40e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 6.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 302 LQTVKLLDLSSNQLIdenqlyliAHLPRLEQLILSDTGISSLhfPDAgigckTSMFPSLKYLVVNDNQISqwSFFNELEK 381
Cdd:COG4886   95 LTNLTELDLSGNEEL--------SNLTNLESLDLSGNQLTDL--PEE-----LANLTNLKELDLSNNQLT--DLPEPLGN 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568215736 382 LPSLRALSCLRNPLTKEDKEaetarlliIASIGQLKTL----NKCEILPEE 428
Cdd:COG4886  158 LTNLKSLDLSNNQLTDLPEE--------LGNLTNLKELdlsnNQITDLPEP 200
LRR_9 pfam14580
Leucine-rich repeat;
284-447 2.58e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 45.14  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736  284 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 363
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736  364 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRkafGNE 443
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166


                  ....
gi 568215736  444 WKQA 447
Cdd:pfam14580 167 GKQL 170
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 499-577 6.80e-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: 41.04  E-value: 6.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568215736 499 LKIKYPhqlDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYespkkpgREIELENDlKSLQFYSVENGDCLLVR 577
Cdd:cd17039    1 ITVKTL---DGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 507-576 3.32e-04

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


Pssm-ID: 405277  Cd Length: 83  Bit Score: 39.43  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568215736  507 LDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKkpGREI-ELENDLKSLQFYSVENGDCLLV 576
Cdd:pfam14560  10 TKAVSSERRFDKSLTIEELKEKLELITGTPPSSMRLQLYDDD--DNLVaKLDDDDALLGSYGVRDGMRIHV 78
LRR_8 pfam13855
Leucine rich repeat;
280-340 6.67e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 6.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568215736  280 PGLEELYLESNNI-FISERPTDVLQTVKLLDLSSNQL--IDENQLyliAHLPRLEQLILSDTGI 340
Cdd:pfam13855   1 PNLRSLDLSNNRLtSLDDGAFKGLSNLKVLDLSNNLLttLSPGAF---SGLPSLRYLDLSGNRL 61
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 497-572 1.47e-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: 37.62  E-value: 1.47e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568215736   497 LTLKIKyphQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYEspkkpGREIElenDLKSLQFYSVENGD 572
Cdd:smart00213   1 IELTVK---TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
282-428 5.99e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.15  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568215736 282 LEELYLESNNIFISERPTDVLQTVKLLDLSSNQLIDENQLYLIAHLPRLEQLILSDT-GISSLhfpdagigcktsmfPSL 360
Cdd:COG4886   50 TLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNeELSNL--------------TNL 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568215736 361 KYLVVNDNQISqwSFFNELEKLPSLRALSCLRNPLTKedkeaetarllIIASIGQLKTL-------NKCEILPEE 428
Cdd:COG4886  116 ESLDLSGNQLT--DLPEELANLTNLKELDLSNNQLTD-----------LPEPLGNLTNLksldlsnNQLTDLPEE 177
 
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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