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Conserved domains on  [gi|4507375|ref|NP_003184|]
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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

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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; ...
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 4507375  444 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 523
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80

                ...
gi 4507375  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 4507375     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 4507375  113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886  82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  193 FPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDEN 268
Cdd:COG4886 150 DLPEPL--GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP 223
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507375  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 4507375  444 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 523
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80

                ...
gi 4507375  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 4507375     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 4507375      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 4507375  113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886  82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  193 FPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDEN 268
Cdd:COG4886 150 DLPEPL--GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP 223
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507375  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 4507375  152 CPNIRKVDLSKNLLSSWDEVihiaDQLRHLEVLNVSENKLkfpsgSVLTG--TLSVLKVLVLNQTGITwaeVLRCVAGCP 229
Cdd:cd21340  23 CKNLKVLYLYDNKITKIENL----EFLTNLTHLYLQNNQI-----EKIENleNLVNLKKLYLGGNRIS---VVEGLENLT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  230 GLEELYLESNNIFISER-------PTDVLQTVKLLDLSSNQLIDENQLyliAHLPRLEQLILSdtgisslhfpdagigck 302
Cdd:cd21340  91 NLEELHIENQRLPPGEKltfdprsLAALSNSLRVLNISGNNIDSLEPL---APLRNLEQLDAS----------------- 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507375  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 4507375   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 4507375   152 CPNIRKV---DLS-KNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITwAEVLRcvAG 227
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPR--GS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375   228 CPGLEELYLeSNNIFISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDTGISslhfpdAGIGCKTSM 305
Cdd:PLN00113 139 IPNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507375   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 4507375    233 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 312
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375    313 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRkafGNE 392
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166

                  ....
gi 4507375    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 4507375    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 4507375     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 4507375  444 QLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPKKPGREIELENDLKSLQFYSVENGDCL 523
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80

                ...
gi 4507375  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 4507375     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 4507375      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 4507375  113 TIGFDSIMKQQSQLSKLQEVSLRNCAVScagekggvaEACPNIRKVDLSKNLLSSWDEVIHiadQLRHLEVLNVSENKLK 192
Cdd:COG4886  82 LSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGNQLTDLPEELA---NLTNLKELDLSNNQLT 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  193 FPSGSVltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQL--IDEN 268
Cdd:COG4886 150 DLPEPL--GNLTNLKSLDLSNNQLT--DLPEELGNLTNLKELDLSNNQI--TDLPEPLgnLTNLEELDLSGNQLtdLPEP 223
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507375  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 4507375  124 SQLSKLQEVSLRNCAVSCAGEKggvAEACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLK-FPSGSvltGT 202
Cdd:COG4886 110 SNLTNLESLDLSGNQLTDLPEE---LANLTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTdLPEEL---GN 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  203 LSVLKVLVLNQTGIT-WAEVLrcvAGCPGLEELYLESNNIfiSERPTDV--LQTVKLLDLSSNQLIDenqLYLIAHLPRL 279
Cdd:COG4886 181 LTNLKELDLSNNQITdLPEPL---GNLTNLEELDLSGNQL--TDLPEPLanLTNLETLDLSNNQLTD---LPELGNLTNL 252
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  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 4507375  119 IMKQQSQLSKLQEVSLRNCAVSCAGEKGGVAEACPNIRKVDLSKNLLSSwdevihiadQLRHLEVLNVSENKLKFPSGSV 198
Cdd:COG4886  62 LSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS---------NLTNLESLDLSGNQLTDLPEEL 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  199 ltGTLSVLKVLVLNQTGITwaEVLRCVAGCPGLEELYLESNNIfiSERPTDVLQTVKL--LDLSSNQLIDENQLylIAHL 276
Cdd:COG4886 133 --ANLTNLKELDLSNNQLT--DLPEPLGNLTNLKSLDLSNNQL--TDLPEELGNLTNLkeLDLSNNQITDLPEP--LGNL 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  277 PRLEQLILSDTGISSLhfPDAGIGCKtsmfpSLKYLVVNDNQISQWSffnELEKLPSLRALSCLRNPLTKEDKEAETARL 356
Cdd:COG4886 205 TNLEELDLSGNQLTDL--PEPLANLT-----NLETLDLSNNQLTDLP---ELGNLTNLEELDLSNNQLTDLPPLANLTNL 274
                       250
                ....*....|....
gi 4507375  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 4507375  152 CPNIRKVDLSKNLLSSWDEVihiaDQLRHLEVLNVSENKLkfpsgSVLTG--TLSVLKVLVLNQTGITwaeVLRCVAGCP 229
Cdd:cd21340  23 CKNLKVLYLYDNKITKIENL----EFLTNLTHLYLQNNQI-----EKIENleNLVNLKKLYLGGNRIS---VVEGLENLT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  230 GLEELYLESNNIFISER-------PTDVLQTVKLLDLSSNQLIDENQLyliAHLPRLEQLILSdtgisslhfpdagigck 302
Cdd:cd21340  91 NLEELHIENQRLPPGEKltfdprsLAALSNSLRVLNISGNNIDSLEPL---APLRNLEQLDAS----------------- 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507375  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 4507375  116 FDSIMKQQSQLSKLQEVSLRNCAVSCAGEkggVAEACPNIRKVDLSKNLLSSWDEVIhiaDQLRHLEVLNVSENKLKFPS 195
Cdd:COG4886 148 LTDLPEPLGNLTNLKSLDLSNNQLTDLPE---ELGNLTNLKELDLSNNQITDLPEPL---GNLTNLEELDLSGNQLTDLP 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  196 GSVltGTLSVLKVLVLNQTGITwaeVLRCVAGCPGLEELYLESNNIfISERPTDVLQTVKLLDLSSNQLIDENqlylIAH 275
Cdd:COG4886 222 EPL--ANLTNLETLDLSNNQLT---DLPELGNLTNLEELDLSNNQL-TDLPPLANLTNLKTLDLSNNQLTDLK----LKE 291
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507375  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 4507375   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 4507375  178 LRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITWAEVLRCVAGCPGLEELYLESNNIFISERPTDVLQTVKLL 257
Cdd:COG4886  14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  258 DLSSNQLIDENQLYLIAHLPRLEQLILSDTGISSLhfPDAgigckTSMFPSLKYLVVNDNQISqwSFFNELEKLPSLRAL 337
Cdd:COG4886  94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDL--PEE-----LANLTNLKELDLSNNQLT--DLPEPLGNLTNLKSL 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4507375  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 4507375  124 SQLSKLQEVSLRNCAVSCAGEK---GGVAEACPNIRKVDLSKNLLSSwDEVIHIADQLRH---LEVLNVSENKLKFPSGS 197
Cdd:cd00116 105 LRSSSLQELKLNNNGLGDRGLRllaKGLKDLPPALEKLVLGRNRLEG-ASCEALAKALRAnrdLKELNLANNGIGDAGIR 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  198 VLTGTL---SVLKVLVLNQTGITWAEVLR---CVAGCPGLEELYLESNNifISERPT--------DVLQTVKLLDLSSNQ 263
Cdd:cd00116 184 ALAEGLkanCNLEVLDLNNNGLTDEGASAlaeTLASLKSLEVLNLGDNN--LTDAGAaalasallSPNISLLTLSLSCND 261

                ....
gi 4507375  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 4507375   152 CPNIRKV---DLS-KNLLSSWDEVIHiadQLRHLEVLNVSENKLKFPSGSVLTGTLSVLKVLVLNQTGITwAEVLRcvAG 227
Cdd:PLN00113  65 CNNSSRVvsiDLSgKNISGKISSAIF---RLPYIQTINLSNNQLSGPIPDDIFTTSSSLRYLNLSNNNFT-GSIPR--GS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375   228 CPGLEELYLeSNNIFISERPTDV--LQTVKLLDLSSNQLIDENQLYlIAHLPRLEQLILSDTGISslhfpdAGIGCKTSM 305
Cdd:PLN00113 139 IPNLETLDL-SNNMLSGEIPNDIgsFSSLKVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLV------GQIPRELGQ 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507375   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 4507375    233 ELYLESNNIFISERPTDVLQTVKLLDLSSNQLideNQLYLIAHLPRLEQLILSDTGISSLhfpDAGIGcktSMFPSLKYL 312
Cdd:pfam14580  23 ELDLRGYKIPIIENLGATLDQFDTIDFSDNEI---RKLDGFPLLRRLKTLLLNNNRICRI---GEGLG---EALPNLTEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375    313 VVNDNQISQWSFFNELEKLPSLRALSCLRNPLTKEdkeaETARLLIIASIGQLKTLNKCEILPEERRRAELDYRkafGNE 392
Cdd:pfam14580  94 ILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNK----PHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFR---SKQ 166

                  ....
gi 4507375    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 4507375  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 4507375    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 4507375    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 4507375  102 QIVTIGNKPVETIGFDSIMKQQSQLSKLQEVSLRNCAVscaGEKG--GVAEA---CPNIRKVDLSKNLLSSwDEVIHIAD 176
Cdd:COG5238 183 ETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPI---GDEGaeILAEAlkgNKSLTTLDLSNNQIGD-EGVIALAE 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  177 QLR-------------------------------HLEVLNVSENKLKFPSGSVLTGTL---SVLKVLVLNQTGITWAEVL 222
Cdd:COG5238 259 ALKnnttvetlylsgnqigaegaialakalqgntTLTSLDLSVNRIGDEGAIALAEGLqgnKTLHTLNLAYNGIGAQGAI 338
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507375  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 4507375  143 GEKG--GVAEA---CPNIRKVDLSKNLLSswDE-VIHIADQLRH---LEVLNVSENKLKfPSGSVLTG-------TLSVL 206
Cdd:COG5238 277 GAEGaiALAKAlqgNTTLTSLDLSVNRIG--DEgAIALAEGLQGnktLHTLNLAYNGIG-AQGAIALAkalqentTLHSL 353
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  207 KvLVLNQTGITWAEVL-RCVAGCPGLEELYLESNNIFISERPT--DVLQTVKL--LDLSSNQLIDENQLYLIAHLPRLEQ 281
Cdd:COG5238 354 D-LSDNQIGDEGAIALaKYLEGNTTLRELNLGKNNIGKQGAEAliDALQTNRLhtLILDGNLIGAEAQQRLEQLLERIKS 432

                .
gi 4507375  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 4507375     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 4507375  126 LSKLQEVSLRNCAVSCAGekggvaeacpnirkVDLSKNLLSSWdevihiadQLRHLEVLNVSENKLKFP-SGSVLTGTLS 204
Cdd:cd00116  80 GCGLQELDLSDNALGPDG--------------CGVLESLLRSS--------SLQELKLNNNGLGDRGLRlLAKGLKDLPP 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  205 VLKVLVLNQTGIT------WAEVLRCVagcPGLEELYLESNNifISERPTDVL-------QTVKLLDLSSNQLIDENQLY 271
Cdd:cd00116 138 ALEKLVLGRNRLEgasceaLAKALRAN---RDLKELNLANNG--IGDAGIRALaeglkanCNLEVLDLNNNGLTDEGASA 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507375  272 L---IAHLPRLEQLILSDTGISS---LHFPDAGIgcktSMFPSLKYLVVNDNQISQWSFFNELEKL---PSLRALSCLRN 342
Cdd:cd00116 213 LaetLASLKSLEVLNLGDNNLTDagaAALASALL----SPNISLLTLSLSCNDITDDGAKDLAEVLaekESLLELDLRGN 288

                ....*...
gi 4507375  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.
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