NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|118442828|ref|NP_001072983|]
View 

tubulin-specific chaperone E isoform a [Homo sapiens]

Protein Classification

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

protein containing domains CAP_GLY, PPP1R42, and Ubl_TBCE

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 444-526 1.06e-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: 125.39  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 444 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 523
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 118442828 524 LVR 526
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 1.09e-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: 1.09e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828   10 IGRRVEVNGEH-ATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 75
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-345 6.98e-16

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 193 FPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDEN 268
Cdd:COG4886  150 DLPEPL--GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828 269 qlylIAHLPRLEQLILSDTGISSLhfpdAGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 345
Cdd:COG4886  224 ----LANLTNLETLDLSNNQLTDL----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; ...
 444-526 1.06e-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: 125.39  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 444 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 523
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 118442828 524 LVR 526
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 1.09e-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: 1.09e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828   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 2.89e-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: 2.89e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442828    10 IGRRVEV--NGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-345 6.98e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 193 FPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDEN 268
Cdd:COG4886  150 DLPEPL--GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828 269 qlylIAHLPRLEQLILSDTGISSLhfpdAGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 345
Cdd:COG4886  224 ----LANLTNLETLDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 152-379 1.38e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 61.34  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 152 CPNIRKVDLSKNLLSSWDEVihiaDQLRHLEVLNVSENKLkfpsgSVLTG--TLSVLKVLVLNQTGITwaeVLRCVAGCP 229
Cdd:cd21340   23 CKNLKVLYLYDNKITKIENL----EFLTNLTHLYLQNNQI-----EKIENleNLVNLKKLYLGGNRIS---VVEGLENLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 230 GLEELYLESNNIFISER-------PTDVLQTVKLLDLSSNQLIDENQLyliAHLPRLEQLILSdtgisslhfpdagigck 302
Cdd:cd21340   91 NLEELHIENQRLPPGEKltfdprsLAALSNSLRVLNISGNNIDSLEPL---APLRNLEQLDAS----------------- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442828 303 tsmfpslkylvvnDNQISQWS-FFNELEKLPSLRALSCLRNPLTKEDKEAETarllIIASIGQLKTLNKCEILPEERR 379
Cdd:cd21340  151 -------------NNQISDLEeLLDLLSSWPSLRELDLTGNPVCKKPKYRDK----IILASKSLEVLDGKEITDTERQ 211
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 7.67e-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: 58.16  E-value: 7.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828  10 IGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTgGSFIRPNKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 152-368 2.99e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.76  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 152 CPNIRKV---DLS-KNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITwAEVLRcvAG 227
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPR--GS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 228 CPGLEELYLeSNNIFISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDTGISslhfpdAGIGCKTSM 305
Cdd:PLN00113 139 IPNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442828 306 FPSLKYLVVNDNQISQwSFFNELEKLPSLRALSCLRNPLTKEdkeaetarllIIASIGQLKTL 368
Cdd:PLN00113 211 MKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLTGP----------IPSSLGNLKNL 262
LRR_9 pfam14580
Leucine-rich repeat;
233-396 3.55e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.37  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828  233 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 312
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828  313 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRkafGNE 392
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166


                  ....
gi 118442828  393 WKQA 396
Cdd:pfam14580 167 GKQL 170
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 456-525 2.89e-04

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


Pssm-ID: 405277  Cd Length: 83  Bit Score: 39.82  E-value: 2.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118442828  456 LDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKkpGREI-ELENDLKSLQFYSVENGDCLLV 525
Cdd:pfam14560  10 TKAVSSERRFDKSLTIEELKEKLELITGTPPSSMRLQLYDDD--DNLVaKLDDDDALLGSYGVRDGMRIHV 78
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 446-521 1.59e-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: 37.24  E-value: 1.59e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118442828   446 LTLKIKyphQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYEspkkpGREIElenDLKSLQFYSVENGD 521
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; ...
 444-526 1.06e-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: 125.39  E-value: 1.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 444 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 523
Cdd:cd17044    1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                 ...
gi 118442828 524 LVR 526
Cdd:cd17044   81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-75 1.09e-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: 1.09e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828   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 2.89e-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: 2.89e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442828    10 IGRRVEV--NGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFKCRhPTGGSFIRPNKV 75
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
113-345 6.98e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 193 FPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDEN 268
Cdd:COG4886  150 DLPEPL--GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828 269 qlylIAHLPRLEQLILSDTGISSLhfpdAGIGCktsmFPSLKYLVVNDNQISQwsfFNELEKLPSLRALSCLRNPLT 345
Cdd:COG4886  224 ----LANLTNLETLDLSNNQLTDL----PELGN----LTNLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLT 285
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-359 2.89e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.67  E-value: 2.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 124 SQLSKLQEVSLRNCAVSCAGEKggvAEACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLK-FPSGSvltGT 202
Cdd:COG4886  110 SNLTNLESLDLSGNQLTDLPEE---LANLTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTdLPEEL---GN 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 203 LSVLKVLVLNQTGIT-WAEVLrcvAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQLIDenqLYLIAHLPRL 279
Cdd:COG4886  181 LTNLKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQL--TDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNL 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 280 EQLILSDTGISSLHfpdagigcKTSMFPSLKYLVVNDNQISQWSffneLEKLPSLRALSCLRNPLTKEDKEAETARLLII 359
Cdd:COG4886  253 EELDLSNNQLTDLP--------PLANLTNLKTLDLSNNQLTDLK----LKELELLLGLNSLLLLLLLLNLLELLILLLLL 320
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
119-369 2.01e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.36  E-value: 2.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 119 IMKQQSQLSKLQEVSLRNCAVSCAGEKGGVAEACPNIRKVDLSKNLLSSwdevihiadQLRHLEVLNVSENKLKFPSGSV 198
Cdd:COG4886   62 LSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS---------NLTNLESLDLSGNQLTDLPEEL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 199 ltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDVLQTVKL--LDLSSNQLIDENQLylIAHL 276
Cdd:COG4886  133 --ANLTNLKELDLSNNQLT--DLPEPLGNLTNLKSLDLSNNQL--TDLPEELGNLTNLkeLDLSNNQITDLPEP--LGNL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 277 PRLEQLILSDTGISSLhfPDAGIGCKtsmfpSLKYLVVNDNQISQWSffnELEKLPSLRALSCLRNPLTKEDKEAETARL 356
Cdd:COG4886  205 TNLEELDLSGNQLTDL--PEPLANLT-----NLETLDLSNNQLTDLP---ELGNLTNLEELDLSNNQLTDLPPLANLTNL 274

                        250
                 ....*....|....
gi 118442828 357 LIIA-SIGQLKTLN 369
Cdd:COG4886  275 KTLDlSNNQLTDLK 288
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 152-379 1.38e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 61.34  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 152 CPNIRKVDLSKNLLSSWDEVihiaDQLRHLEVLNVSENKLkfpsgSVLTG--TLSVLKVLVLNQTGITwaeVLRCVAGCP 229
Cdd:cd21340   23 CKNLKVLYLYDNKITKIENL----EFLTNLTHLYLQNNQI-----EKIENleNLVNLKKLYLGGNRIS---VVEGLENLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 230 GLEELYLESNNIFISER-------PTDVLQTVKLLDLSSNQLIDENQLyliAHLPRLEQLILSdtgisslhfpdagigck 302
Cdd:cd21340   91 NLEELHIENQRLPPGEKltfdprsLAALSNSLRVLNISGNNIDSLEPL---APLRNLEQLDAS----------------- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442828 303 tsmfpslkylvvnDNQISQWS-FFNELEKLPSLRALSCLRNPLTKEDKEAETarllIIASIGQLKTLNKCEILPEERR 379
Cdd:cd21340  151 -------------NNQISDLEeLLDLLSSWPSLRELDLTGNPVCKKPKYRDK----IILASKSLEVLDGKEITDTERQ 211
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
116-343 3.14e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.26  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 116 FDSIMKQQSQLSKLQEVSLRNCAVSCAGEkggVAEACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLKFPS 195
Cdd:COG4886  148 LTDLPEPLGNLTNLKSLDLSNNQLTDLPE---ELGNLTNLKELDLSNNQITDLPEPL---GNLTNLEELDLSGNQLTDLP 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 196 GSVltGTLSVLKVLVLNQTGITwaeVLRCVAGCPGLEELYLESNNIfISERPTDVLQTVKLLDLSSNQLIDENqlylIAH 275
Cdd:COG4886  222 EPL--ANLTNLETLDLSNNQLT---DLPELGNLTNLEELDLSNNQL-TDLPPLANLTNLKTLDLSNNQLTDLK----LKE 291

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442828 276 LPRLEQLILSDTGISSLHFPDAGIGCKTSMFPSLKYLVVNDNQISQWSFFNELEKLPSLRALSCLRNP 343
Cdd:COG4886  292 LELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLL 359
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 10-76 7.67e-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: 58.16  E-value: 7.67e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442828  10 IGRRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPeRGKHDGSHEGTVYFKCRHPTgGSFIRPNKVN 76
Cdd:COG5244    6 VNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPDDDS 70
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
178-377 6.61e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.39  E-value: 6.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 178 LRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITWAEVLRCVAGCPGLEELYLESNNIFISERPTDVLQTVKLL 257
Cdd:COG4886   14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 258 DLSSNQLIDENQLYLIAHLPRLEQLILSDTGISSLhfPDAgigckTSMFPSLKYLVVNDNQISqwSFFNELEKLPSLRAL 337
Cdd:COG4886   94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDL--PEE-----LANLTNLKELDLSNNQLT--DLPEPLGNLTNLKSL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 118442828 338 SCLRNPLTKEDKEaetarlliIASIGQLKTL----NKCEILPEE 377
Cdd:COG4886  165 DLSNNQLTDLPEE--------LGNLTNLKELdlsnNQITDLPEP 200
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 124-267 1.88e-05

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.58  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 124 SQLSKLQEVSLRNCAVSCAGEK---GGVAEACPNIRKVDLSKNLLSSwDEVIHIADQLRH---LEVLNVSENKLKFPSGS 197
Cdd:cd00116  105 LRSSSLQELKLNNNGLGDRGLRllaKGLKDLPPALEKLVLGRNRLEG-ASCEALAKALRAnrdLKELNLANNGIGDAGIR 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 198 VLTGTL---SVLKVLVLNQTGITWAEVLR---CVAGCPGLEELYLESNNifISERPT--------DVLQTVKLLDLSSNQ 263
Cdd:cd00116  184 ALAEGLkanCNLEVLDLNNNGLTDEGASAlaeTLASLKSLEVLNLGDNN--LTDAGAaalasallSPNISLLTLSLSCND 261


                 ....
gi 118442828 264 LIDE 267
Cdd:cd00116  262 ITDD 265
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 152-368 2.99e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.76  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 152 CPNIRKV---DLS-KNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITwAEVLRcvAG 227
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPR--GS 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 228 CPGLEELYLeSNNIFISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDTGISslhfpdAGIGCKTSM 305
Cdd:PLN00113 139 IPNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442828 306 FPSLKYLVVNDNQISQwSFFNELEKLPSLRALSCLRNPLTKEdkeaetarllIIASIGQLKTL 368
Cdd:PLN00113 211 MKSLKWIYLGYNNLSG-EIPYEIGGLTSLNHLDLVYNNLTGP----------IPSSLGNLKNL 262
LRR_9 pfam14580
Leucine-rich repeat;
233-396 3.55e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.37  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828  233 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 312
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828  313 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRkafGNE 392
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166


                  ....
gi 118442828  393 WKQA 396
Cdd:pfam14580 167 GKQL 170
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 448-526 7.30e-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: 7.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442828 448 LKIKYPhqlDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYespkkpgREIELENDlKSLQFYSVENGDCLLVR 526
Cdd:cd17039    1 ITVKTL---DGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIY-------NGKELKDD-KTLSDYGIKDGSTIHLV 68
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 456-525 2.89e-04

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


Pssm-ID: 405277  Cd Length: 83  Bit Score: 39.82  E-value: 2.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118442828  456 LDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKkpGREI-ELENDLKSLQFYSVENGDCLLV 525
Cdd:pfam14560  10 TKAVSSERRFDKSLTIEELKEKLELITGTPPSSMRLQLYDDD--DNLVaKLDDDDALLGSYGVRDGMRIHV 78
LRR_8 pfam13855
Leucine rich repeat;
229-289 9.17e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 9.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118442828  229 PGLEELYLESNNI-FISERPTDVLQTVKLLDLSSNQL--IDENQLyliAHLPRLEQLILSDTGI 289
Cdd:pfam13855   1 PNLRSLDLSNNRLtSLDDGAFKGLSNLKVLDLSNNLLttLSPGAF---SGLPSLRYLDLSGNRL 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 102-289 9.64e-04

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: 41.70  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 102 QIVTIGNKPVETIGFDSIMKQQSQLSKLQEVSLRNCAVscaGEKG--GVAEA---CPNIRKVDLSKNLLSSwDEVIHIAD 176
Cdd:COG5238  183 ETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPI---GDEGaeILAEAlkgNKSLTTLDLSNNQIGD-EGVIALAE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 177 QLR-------------------------------HLEVLNVSENKLKFPSGSVLTGTL---SVLKVLVLNQTGITWAEVL 222
Cdd:COG5238  259 ALKnnttvetlylsgnqigaegaialakalqgntTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIGAQGAI 338

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442828 223 RCVAGC---PGLEELYLESNNIfiSERPTDVL-------QTVKLLDLSSNQLIDENQLYLIAHL--PRLEQLILSDTGI 289
Cdd:COG5238  339 ALAKALqenTTLHSLDLSDNQI--GDEGAIALakylegnTTLRELNLGKNNIGKQGAEALIDALqtNRLHTLILDGNLI 415
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 143-282 1.56e-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: 40.93  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 143 GEKG--GVAEA---CPNIRKVDLSKNLLSswDE-VIHIADQLRH---LEVLNVSENKLKfPSGSVLTG-------TLSVL 206
Cdd:COG5238  277 GAEGaiALAKAlqgNTTLTSLDLSVNRIG--DEgAIALAEGLQGnktLHTLNLAYNGIG-AQGAIALAkalqentTLHSL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 207 KvLVLNQTGITWAEVL-RCVAGCPGLEELYLESNNIFISERPT--DVLQTVKL--LDLSSNQLIDENQLYLIAHLPRLEQ 281
Cdd:COG5238  354 D-LSDNQIGDEGAIALaKYLEGNTTLRELNLGKNNIGKQGAEAliDALQTNRLhtLILDGNLIGAEAQQRLEQLLERIKS 432


                 .
gi 118442828 282 L 282
Cdd:COG5238  433 V 433
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 446-521 1.59e-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: 37.24  E-value: 1.59e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118442828   446 LTLKIKyphQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYEspkkpGREIElenDLKSLQFYSVENGD 521
Cdd:smart00213   1 IELTVK---TLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYK-----GKVLE---DDRTLADYGIQDGS 65
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 126-350 7.06e-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: 38.49  E-value: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 126 LSKLQEVSLRNCAVSCAGekggvaeacpnirkVDLSKNLLSSWdevihiadQLRHLEVLNVSENKLKFP-SGSVLTGTLS 204
Cdd:cd00116   80 GCGLQELDLSDNALGPDG--------------CGVLESLLRSS--------SLQELKLNNNGLGDRGLRlLAKGLKDLPP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 205 VLKVLVLNQTGIT------WAEVLRCVagcPGLEELYLESNNifISERPTDVL-------QTVKLLDLSSNQLIDENQLY 271
Cdd:cd00116  138 ALEKLVLGRNRLEgasceaLAKALRAN---RDLKELNLANNG--IGDAGIRALaeglkanCNLEVLDLNNNGLTDEGASA 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442828 272 L---IAHLPRLEQLILSDTGISS---LHFPDAGIgcktSMFPSLKYLVVNDNQISQWSFFNELEKL---PSLRALSCLRN 342
Cdd:cd00116  213 LaetLASLKSLEVLNLGDNNLTDagaAALASALL----SPNISLLTLSLSCNDITDDGAKDLAEVLaekESLLELDLRGN 288


                 ....*...
gi 118442828 343 PLTKEDKE 350
Cdd:cd00116  289 KFGEEGAQ 296
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH