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Conserved domains on  [gi|529010368|ref|XP_005226263|]
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tubulin-specific chaperone E isoform X1 [Bos taurus]

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; ...
 445-527 1.87e-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: 124.61  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 445 QLLTLKIKYPNQHDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESPKMPGKEVELENDLQPLRFYSVENGDCL 524
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 529010368 525 LVR 527
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 3.22e-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: 98.24  E-value: 3.22e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529010368   10 IGRRVEVNGEH-ATVRFSGLVPPVAGLWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTAGSFIRPHKV 75
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-320 1.87e-13

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 72.27  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 124 SQLSKLQDVSLRNCAVNGAGDkgEIAKaCPNIRSIDLSKNLLSSWEEVIdiaDQLKHLEVLNLSENKLTSPSSSPsptGT 203
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPE--ELAN-LTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTDLPEEL---GN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 204 FPTLKVLVLNRTGVT-WAEVLrcaSGWPVLEKLYLESNNiiISERPTDV--LQTVKLLDLSSNQLIDenqLFLIAYLPRL 280
Cdd:COG4886  181 LTNLKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQ--LTDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNL 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 529010368 281 EQLILSDIGISSIHfpdagigcKTSMFPSLQYLVLNDNQI 320
Cdd:COG4886  253 EELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQL 284
LRR_9 super family cl25994
Leucine-rich repeat;
258-396 2.89e-05

Leucine-rich repeat;


The actual alignment was detected with superfamily member pfam14580:

Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.75  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368  258 LDLSSNQLideNQLFLIAYLPRLEQLILSDIGISSIhfpDAGIGcktSMFPSLQYLVLNDNQIAQWSFMNELDKLQSLHA 337
Cdd:pfam14580  47 IDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTELILTNNNLQELGDLDPLASLKKLTF 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 529010368  338 LSCTRNPLTegskDAQTTRQFIIARIGQLRTLNKCAIEPEERRGAELDYRKAFGNEWKK 396
Cdd:pfam14580 118 LSLLRNPVT----NKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGKQLAK 172
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 445-527 1.87e-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: 124.61  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 445 QLLTLKIKYPNQHDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESPKMPGKEVELENDLQPLRFYSVENGDCL 524
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 529010368 525 LVR 527
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 3.22e-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: 98.24  E-value: 3.22e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529010368   10 IGRRVEVNGEH-ATVRFSGLVPPVAGLWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTAGSFIRPHKV 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 5.40e-25

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 98.04  E-value: 5.40e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529010368    10 IGRRVEV--NGEHATVRFSGLVPPVAGLWLGVEWDNPERGKHDGSHEGTVYFKCRhPTAGSFIRPHKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-320 1.87e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 72.27  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 124 SQLSKLQDVSLRNCAVNGAGDkgEIAKaCPNIRSIDLSKNLLSSWEEVIdiaDQLKHLEVLNLSENKLTSPSSSPsptGT 203
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPE--ELAN-LTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTDLPEEL---GN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 204 FPTLKVLVLNRTGVT-WAEVLrcaSGWPVLEKLYLESNNiiISERPTDV--LQTVKLLDLSSNQLIDenqLFLIAYLPRL 280
Cdd:COG4886  181 LTNLKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQ--LTDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNL 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 529010368 281 EQLILSDIGISSIHfpdagigcKTSMFPSLQYLVLNDNQI 320
Cdd:COG4886  253 EELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQL 284
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 1.01e-08

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: 57.77  E-value: 1.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529010368  10 IGRRVEVNGEHATVRFSGLVPPVAGLWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTaGSFIRPHKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 232-380 2.73e-06

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 48.24  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 232 LEKLYLESNNI-IIS--ERPTDvLQTvklLDLSSNQLIDENQLF-----LIAYLPRLEQLILSDIGISSIhfpdAGIGCk 303
Cdd:cd21340   70 LKKLYLGGNRIsVVEglENLTN-LEE---LHIENQRLPPGEKLTfdprsLAALSNSLRVLNISGNNIDSL----EPLAP- 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529010368 304 tsmFPSLQYLVLNDNQIAQWS-FMNELDKLQSLHALSCTRNPLTEGSKdaqtTRQFIIARIGQLRTLNKCAIEPEERR 380
Cdd:cd21340  141 ---LRNLEQLDASNNQISDLEeLLDLLSSWPSLRELDLTGNPVCKKPK----YRDKIILASKSLEVLDGKEITDTERQ 211
LRR_9 pfam14580
Leucine-rich repeat;
258-396 2.89e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.75  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368  258 LDLSSNQLideNQLFLIAYLPRLEQLILSDIGISSIhfpDAGIGcktSMFPSLQYLVLNDNQIAQWSFMNELDKLQSLHA 337
Cdd:pfam14580  47 IDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTELILTNNNLQELGDLDPLASLKKLTF 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 529010368  338 LSCTRNPLTegskDAQTTRQFIIARIGQLRTLNKCAIEPEERRGAELDYRKAFGNEWKK 396
Cdd:pfam14580 118 LSLLRNPVT----NKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGKQLAK 172
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 447-522 2.49e-04

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: 39.55  E-value: 2.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529010368   447 LTLKIKypnQHDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEspkmpGKevELENDlQPLRFYSVENGD 522
Cdd:smart00213   1 IELTVK---TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GK--VLEDD-RTLADYGIQDGS 65
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 153-191 9.58e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.14  E-value: 9.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 529010368  153 PNIRSIDLSKNLLSSweevIDIADQLKHLEVLNLSENKL 191
Cdd:pfam12799   1 PNLEVLDLSNNQITD----IPPLAKLPNLETLDLSGNNK 35
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 445-527 1.87e-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: 124.61  E-value: 1.87e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 445 QLLTLKIKYPNQHDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYESPKMPGKEVELENDLQPLRFYSVENGDCL 524
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 529010368 525 LVR 527
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 3.22e-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: 98.24  E-value: 3.22e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529010368   10 IGRRVEVNGEH-ATVRFSGLVPPVAGLWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTAGSFIRPHKV 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 5.40e-25

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 98.04  E-value: 5.40e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529010368    10 IGRRVEV--NGEHATVRFSGLVPPVAGLWLGVEWDNPERGKHDGSHEGTVYFKCRhPTAGSFIRPHKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-320 1.87e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 72.27  E-value: 1.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 124 SQLSKLQDVSLRNCAVNGAGDkgEIAKaCPNIRSIDLSKNLLSSWEEVIdiaDQLKHLEVLNLSENKLTSPSSSPsptGT 203
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPE--ELAN-LTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTDLPEEL---GN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 204 FPTLKVLVLNRTGVT-WAEVLrcaSGWPVLEKLYLESNNiiISERPTDV--LQTVKLLDLSSNQLIDenqLFLIAYLPRL 280
Cdd:COG4886  181 LTNLKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQ--LTDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNL 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 529010368 281 EQLILSDIGISSIHfpdagigcKTSMFPSLQYLVLNDNQI 320
Cdd:COG4886  253 EELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
154-347 1.47e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 154 NIRSIDLSKNLLSSWEEVIDIADQLKHLEVLNLSENKltspssspsPTGTFPTLKVLVLNRTGVTwaEVLRCASGWPVLE 233
Cdd:COG4886   71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE---------ELSNLTNLESLDLSGNQLT--DLPEELANLTNLK 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 234 KLYLESNNIiiSERPTDV--LQTVKLLDLSSNQL--IDENqlflIAYLPRLEQLILSDIGISSIHFPdagIGCktsmFPS 309
Cdd:COG4886  140 ELDLSNNQL--TDLPEPLgnLTNLKSLDLSNNQLtdLPEE----LGNLTNLKELDLSNNQITDLPEP---LGN----LTN 206

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 529010368 310 LQYLVLNDNQIAqwSFMNELDKLQSLHALSCTRNPLTE 347
Cdd:COG4886  207 LEELDLSGNQLT--DLPEPLANLTNLETLDLSNNQLTD 242
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-344 2.12e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.64  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 124 SQLSKLQDVSLRNCAVNGAGDkgEIAKaCPNIRSIDLSKNLLSSWEEVIDiadQLKHLEVLNLSENKLTSPSSSPsptGT 203
Cdd:COG4886  156 GNLTNLKSLDLSNNQLTDLPE--ELGN-LTNLKELDLSNNQITDLPEPLG---NLTNLEELDLSGNQLTDLPEPL---AN 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 204 FPTLKVLVLNRTGVTWAEVLrcaSGWPVLEKLYLeSNNIIISERPTDVLQTVKLLDLSSNQLIDENqlflIAYLPRLEQL 283
Cdd:COG4886  227 LTNLETLDLSNNQLTDLPEL---GNLTNLEELDL-SNNQLTDLPPLANLTNLKTLDLSNNQLTDLK----LKELELLLGL 298

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529010368 284 ILSDIGISSIHFPDAGIGCKTSMFPSLQYLVLNDNQIAQWSFMNELDKLQSLHALSCTRNP 344
Cdd:COG4886  299 NSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLL 359
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 1.01e-08

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: 57.77  E-value: 1.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529010368  10 IGRRVEVNGEHATVRFSGLVPPVAGLWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTaGSFIRPHKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 232-380 2.73e-06

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 48.24  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 232 LEKLYLESNNI-IIS--ERPTDvLQTvklLDLSSNQLIDENQLF-----LIAYLPRLEQLILSDIGISSIhfpdAGIGCk 303
Cdd:cd21340   70 LKKLYLGGNRIsVVEglENLTN-LEE---LHIENQRLPPGEKLTfdprsLAALSNSLRVLNISGNNIDSL----EPLAP- 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529010368 304 tsmFPSLQYLVLNDNQIAQWS-FMNELDKLQSLHALSCTRNPLTEGSKdaqtTRQFIIARIGQLRTLNKCAIEPEERR 380
Cdd:cd21340  141 ---LRNLEQLDASNNQISDLEeLLDLLSSWPSLRELDLTGNPVCKKPK----YRDKIILASKSLEVLDGKEITDTERQ 211
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 449-527 5.49e-06

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: 44.12  E-value: 5.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529010368 449 LKIKYPnqhDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYespkmpgKEVELENDlQPLRFYSVENGDCLLVR 527
Cdd:cd17039    1 ITVKTL---DGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 102-294 1.02e-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: 47.86  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 102 QIVIIGNKPVETIGFDSVIKQQSQLSKLQDVSLRNcavNGAGDKG--EIAKA---CPNIRSIDLSKNLLSSwEEVIDIAD 176
Cdd:COG5238  183 ETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKR---NPIGDEGaeILAEAlkgNKSLTTLDLSNNQIGD-EGVIALAE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 177 QLKH---LEVLNLSENKLTSPSSSPSPTG--TFPTLKVLVL--NRTG----VTWAEVLRcasGWPVLEKLYLESNNI--- 242
Cdd:COG5238  259 ALKNnttVETLYLSGNQIGAEGAIALAKAlqGNTTLTSLDLsvNRIGdegaIALAEGLQ---GNKTLHTLNLAYNGIgaq 335

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 529010368 243 ----IISERPTDvlQTVKLLDLSSNQLIDENQLFLIAYLPRLEQLILSDIGISSIH 294
Cdd:COG5238  336 gaiaLAKALQEN--TTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIG 389
LRR_9 pfam14580
Leucine-rich repeat;
258-396 2.89e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.75  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368  258 LDLSSNQLideNQLFLIAYLPRLEQLILSDIGISSIhfpDAGIGcktSMFPSLQYLVLNDNQIAQWSFMNELDKLQSLHA 337
Cdd:pfam14580  47 IDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTELILTNNNLQELGDLDPLASLKKLTF 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 529010368  338 LSCTRNPLTegskDAQTTRQFIIARIGQLRTLNKCAIEPEERRGAELDYRKAFGNEWKK 396
Cdd:pfam14580 118 LSLLRNPVT----NKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGKQLAK 172
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 114-283 4.25e-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: 45.94  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 114 IGFDSVIKQQSQLSKLqDVSLRNCAVNGAGDKGEIAKACPNIRSIDLSKNLLSSwEEVIDIADQLKH---LEVLNLSENK 190
Cdd:COG5238  254 IALAEALKNNTTVETL-YLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD-EGAIALAEGLQGnktLHTLNLAYNG 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 191 LTSPSSSPSPTG--TFPTLKVLVL--NRTGVTWAEVLRCA-SGWPVLEKLYLESNNIIISERPT--DVLQTVKL--LDLS 261
Cdd:COG5238  332 IGAQGAIALAKAlqENTTLHSLDLsdNQIGDEGAIALAKYlEGNTTLRELNLGKNNIGKQGAEAliDALQTNRLhtLILD 411

                        170       180
                 ....*....|....*....|..
gi 529010368 262 SNQLIDENQLFLIAYLPRLEQL 283
Cdd:COG5238  412 GNLIGAEAQQRLEQLLERIKSV 433
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
178-370 1.25e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 178 LKHLEVLNLSENKLTSPSSSPSPTGTFPTLKVLVLNRTGVTWAEVLRCASGWPVLEKLYLESNNIIISERPTDVLQTVKL 257
Cdd:COG4886   21 LTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 258 LDLSSNQLIdenqlfliAYLPRLEQLILSDIGISSIhfPDAgigckTSMFPSLQYLVLNDNQIAqwSFMNELDKLQSLHA 337
Cdd:COG4886  101 LDLSGNEEL--------SNLTNLESLDLSGNQLTDL--PEE-----LANLTNLKELDLSNNQLT--DLPEPLGNLTNLKS 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 529010368 338 LSCTRNPLTEGSKDaqttrqfiIARIGQLRTLN 370
Cdd:COG4886  164 LDLSNNQLTDLPEE--------LGNLTNLKELD 188
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 447-522 2.49e-04

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: 39.55  E-value: 2.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529010368   447 LTLKIKypnQHDQKVIEKQLPDSMTVQKVKGLLSRLLKVPVSELLLSYEspkmpGKevELENDlQPLRFYSVENGD 522
Cdd:smart00213   1 IELTVK---TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GK--VLEDD-RTLADYGIQDGS 65
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 124-212 5.49e-03

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 38.88  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 124 SQLSKLQDVSLRNCAVNGAGDK--GEIAKACPNIRSIDLSKNLLSSwEEVIDIADQLKH---LEVLNLSENKLTSPSSSP 198
Cdd:cd00116  162 RANRDLKELNLANNGIGDAGIRalAEGLKANCNLEVLDLNNNGLTD-EGASALAETLASlksLEVLNLGDNNLTDAGAAA 240

                         90
                 ....*....|....*..
gi 529010368 199 SPTG---TFPTLKVLVL 212
Cdd:cd00116  241 LASAllsPNISLLTLSL 257
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-288 5.80e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.15  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 124 SQLSKLQDVSLRNCAVNgagDKGEIAKaCPNIRSIDLSKNLLSSweevIDIADQLKHLEVLNLSENKLTSPSSSPSPTGT 203
Cdd:COG4886  225 ANLTNLETLDLSNNQLT---DLPELGN-LTNLEELDLSNNQLTD----LPPLANLTNLKTLDLSNNQLTDLKLKELELLL 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010368 204 FPTLKVLVLNRTGVTWAEVLRCASGWPVLEKLYLESNNIIISERPTDVLQTVKLLDLSSNQLIDENQLFLIAYLPRLEQL 283
Cdd:COG4886  297 GLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLE 376


                 ....*
gi 529010368 284 ILSDI 288
Cdd:COG4886  377 ATLLT 381
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 153-191 9.58e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.14  E-value: 9.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 529010368  153 PNIRSIDLSKNLLSSweevIDIADQLKHLEVLNLSENKL 191
Cdd:pfam12799   1 PNLEVLDLSNNQITD----IPPLAKLPNLETLDLSGNNK 35
 
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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