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Conserved domains on  [gi|88942576|sp|Q5U378|]
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RecName: Full=Tubulin-specific chaperone E; AltName: Full=Tubulin-folding cofactor E

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; ...
 437-519 1.91e-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: 1.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 437 QLLTITFLCPEDLERKPIEKKLPGSMIVQKVKGLLHRLLKLPGVELKLTYTCAKMADREIEIDNDLKPLQFYSVEDGDKI 516
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                ...
gi 88942576 517 LVR 519
Cdd:cd17044  81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 7-71 3.81e-31

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: 114.81  E-value: 3.81e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88942576     7 VGRRVCCDGER-GTVRYVGPVPPTAGVWLGVEWDHPeRGKHDGSHDGVRYFTCRhPTGGSFVRPQK 71
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSK 64
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
151-364 8.16e-16

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 8.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 151 LDLSGNLLSSWEVLAAITEQLDSLQELHLSHNRLSISSApsslssafsHLRVLSINSCALTwtQVLHCAPMWQQVEELYL 230
Cdd:COG4886  75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLT---------NLESLDLSGNQLT--DLPEELANLTNLKELDL 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 231 ADNNITELLRPEHVLQALTVLDLSNNQIaqeTVL--EISHLPRLERLNLSSTSLSEIK--FSDvpagkkttlFPALKELL 306
Cdd:COG4886 144 SNNQLTDLPEPLGNLTNLKSLDLSNNQL---TDLpeELGNLTNLKELDLSNNQITDLPepLGN---------LTNLEELD 211

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 88942576 307 LDDNNISEwrVVNELEKLPSLVYLSCRRNPLlhkeKNLETarqimIARLGQLELLDMR 364
Cdd:COG4886 212 LSGNQLTD--LPEPLANLTNLETLDLSNNQL----TDLPE-----LGNLTNLEELDLS 258
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 437-519 1.91e-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: 1.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 437 QLLTITFLCPEDLERKPIEKKLPGSMIVQKVKGLLHRLLKLPGVELKLTYTCAKMADREIEIDNDLKPLQFYSVEDGDKI 516
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                ...
gi 88942576 517 LVR 519
Cdd:cd17044  81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 7-71 3.81e-31

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: 114.81  E-value: 3.81e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88942576     7 VGRRVCCDGER-GTVRYVGPVPPTAGVWLGVEWDHPeRGKHDGSHDGVRYFTCRhPTGGSFVRPQK 71
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSK 64
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 7-71 1.14e-29

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: 110.75  E-value: 1.14e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88942576      7 VGRRVCC--DGERGTVRYVGPVPPTAGVWLGVEWDHPERGKHDGSHDGVRYFTCRhPTGGSFVRPQK 71
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSK 66
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
151-364 8.16e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 8.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 151 LDLSGNLLSSWEVLAAITEQLDSLQELHLSHNRLSISSApsslssafsHLRVLSINSCALTwtQVLHCAPMWQQVEELYL 230
Cdd:COG4886  75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLT---------NLESLDLSGNQLT--DLPEELANLTNLKELDL 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 231 ADNNITELLRPEHVLQALTVLDLSNNQIaqeTVL--EISHLPRLERLNLSSTSLSEIK--FSDvpagkkttlFPALKELL 306
Cdd:COG4886 144 SNNQLTDLPEPLGNLTNLKSLDLSNNQL---TDLpeELGNLTNLKELDLSNNQITDLPepLGN---------LTNLEELD 211

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 88942576 307 LDDNNISEwrVVNELEKLPSLVYLSCRRNPLlhkeKNLETarqimIARLGQLELLDMR 364
Cdd:COG4886 212 LSGNQLTD--LPEPLANLTNLETLDLSNNQL----TDLPE-----LGNLTNLEELDLS 258
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 216-372 5.62e-11

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: 62.50  E-value: 5.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 216 LHCAPmwqQVEELYLADNNITELlRPEHVLQALTVLDLSNNQIA-----------QETVLE-----------------IS 267
Cdd:cd21340  42 LEFLT---NLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISvveglenltnlEELHIEnqrlppgekltfdprslAA 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 268 HLPRLERLNLSS---TSLSEIKFsdvpagkkttlFPALKELLLDDNNISEWRVVNE-LEKLPSLVYLSCRRNPLLHKEKN 343
Cdd:cd21340 118 LSNSLRVLNISGnniDSLEPLAP-----------LRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKKPKY 186

                       170       180
                ....*....|....*....|....*....
gi 88942576 344 letaRQIMIARLGQLELLDMRQILSDERR 372
Cdd:cd21340 187 ----RDKIILASKSLEVLDGKEITDTERQ 211
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 6-122 1.05e-10

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: 64.32  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576   6 AVGRRVCCDGERGTVRYVGPVPPTAGVWLGVEWDHPeRGKHDGSHDGVRYFTCRHPTgGSFVRP---------------- 69
Cdd:COG5244   5 SVNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPdddsllngnaayekik 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88942576  70 ---QKASFGVDYVTALKQ---RYEVEIEEVTAEEMKI----SSKTVVMVGFENVKKKQSVKNL 122
Cdd:COG5244  83 gglVCESKGMDKDGEIKQenhEDRIHFEESKIRRLEEtieaLKSTEKEEIVELRRENEELDKI 145
LRR_9 pfam14580
Leucine-rich repeat;
251-384 3.09e-08

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 53.23  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576   251 LDLSNNQIAQetvLE-ISHLPRLERLNLSSTSLSEIKfsdvpAGKKTTLfPALKELLLDDNNISEWRVVNELEKLPSLVY 329
Cdd:pfam14580  47 IDFSDNEIRK---LDgFPLLRRLKTLLLNNNRICRIG-----EGLGEAL-PNLTELILTNNNLQELGDLDPLASLKKLTF 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 88942576   330 LSCRRNPLLHKEKnletARQIMIARLGQLELLDMRQILSDERRGAEldycKMFGS 384
Cdd:pfam14580 118 LSLLRNPVTNKPH----YRLYVIYKVPQLRLLDFRKVKQKERQAAE----KMFRS 164
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
199-361 7.98e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 55.09  E-value: 7.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576  199 HLRVLSINSCALTWTQvlhcAPMWQQVEELYLADNNITELlrPEHVLQALTVLDLSNNQIA--QETVLE----------- 265
Cdd:PRK15370 221 NIKTLYANSNQLTSIP----ATLPDTIQEMELSINRITEL--PERLPSALQSLDLFHNKISclPENLPEelrylsvydns 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576  266 ----ISHLPR-LERLNLSSTSLSEIKfSDVPAGKKT-------------TLFPALKELLLDDNNISewrVVNELEKlPSL 327
Cdd:PRK15370 295 irtlPAHLPSgITHLNVQSNSLTALP-ETLPPGLKTleagenaltslpaSLPPELQVLDVSKNQIT---VLPETLP-PTI 369

                        170       180       190
                 ....*....|....*....|....*....|....
gi 88942576  328 VYLSCRRNPLLHKEKNLETARQIMIARLGQLELL 361
Cdd:PRK15370 370 TTLDVSRNALTNLPENLPAALQIMQASRNNLVRL 403
 
Name Accession Description Interval E-value
Ubl_TBCE cd17044
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor E (TBCE) and similar proteins; ...
 437-519 1.91e-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: 1.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 437 QLLTITFLCPEDLERKPIEKKLPGSMIVQKVKGLLHRLLKLPGVELKLTYTCAKMADREIEIDNDLKPLQFYSVEDGDKI 516
Cdd:cd17044   1 SLITLTLVCPAAPEKKPIEKKLPSSMTVQKLKGLCERLFKLPASKQRLSYVSSEGPGIEIELDDDLRSLSFYSVEDGDTI 80


                ...
gi 88942576 517 LVR 519
Cdd:cd17044  81 LVR 83
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 7-71 3.81e-31

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: 114.81  E-value: 3.81e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88942576     7 VGRRVCCDGER-GTVRYVGPVPPTAGVWLGVEWDHPeRGKHDGSHDGVRYFTCRhPTGGSFVRPQK 71
Cdd:pfam01302   1 VGDRVEVPGGRrGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSK 64
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 7-71 1.14e-29

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: 110.75  E-value: 1.14e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88942576      7 VGRRVCC--DGERGTVRYVGPVPPTAGVWLGVEWDHPERGKHDGSHDGVRYFTCRhPTGGSFVRPQK 71
Cdd:smart01052   1 VGDRVEVggGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSK 66
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
151-364 8.16e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 8.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 151 LDLSGNLLSSWEVLAAITEQLDSLQELHLSHNRLSISSApsslssafsHLRVLSINSCALTwtQVLHCAPMWQQVEELYL 230
Cdd:COG4886  75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLT---------NLESLDLSGNQLT--DLPEELANLTNLKELDL 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 231 ADNNITELLRPEHVLQALTVLDLSNNQIaqeTVL--EISHLPRLERLNLSSTSLSEIK--FSDvpagkkttlFPALKELL 306
Cdd:COG4886 144 SNNQLTDLPEPLGNLTNLKSLDLSNNQL---TDLpeELGNLTNLKELDLSNNQITDLPepLGN---------LTNLEELD 211

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 88942576 307 LDDNNISEwrVVNELEKLPSLVYLSCRRNPLlhkeKNLETarqimIARLGQLELLDMR 364
Cdd:COG4886 212 LSGNQLTD--LPEPLANLTNLETLDLSNNQL----TDLPE-----LGNLTNLEELDLS 258
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
120-317 6.18e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.90  E-value: 6.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 120 KNLTEVGLRRCEVSAPGPEneIRNTTpFVQSLDLSGNLLSS-WEVLAaiteQLDSLQELHLSHNRLSISSAPSSLSSafs 198
Cdd:COG4886 113 TNLESLDLSGNQLTDLPEE--LANLT-NLKELDLSNNQLTDlPEPLG----NLTNLKSLDLSNNQLTDLPEELGNLT--- 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 199 HLRVLSINSCALT-WTQVLHCapmWQQVEELYLADNNITELLRPEHVLQALTVLDLSNNQIaqETVLEISHLPRLERLNL 277
Cdd:COG4886 183 NLKELDLSNNQITdLPEPLGN---LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQL--TDLPELGNLTNLEELDL 257

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 88942576 278 SSTSLSEIKFSdvpagkktTLFPALKELLLDDNNISEWRV 317
Cdd:COG4886 258 SNNQLTDLPPL--------ANLTNLKTLDLSNNQLTDLKL 289
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 216-372 5.62e-11

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: 62.50  E-value: 5.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 216 LHCAPmwqQVEELYLADNNITELlRPEHVLQALTVLDLSNNQIA-----------QETVLE-----------------IS 267
Cdd:cd21340  42 LEFLT---NLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISvveglenltnlEELHIEnqrlppgekltfdprslAA 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 268 HLPRLERLNLSS---TSLSEIKFsdvpagkkttlFPALKELLLDDNNISEWRVVNE-LEKLPSLVYLSCRRNPLLHKEKN 343
Cdd:cd21340 118 LSNSLRVLNISGnniDSLEPLAP-----------LRNLEQLDASNNQISDLEELLDlLSSWPSLRELDLTGNPVCKKPKY 186

                       170       180
                ....*....|....*....|....*....
gi 88942576 344 letaRQIMIARLGQLELLDMRQILSDERR 372
Cdd:cd21340 187 ----RDKIILASKSLEVLDGKEITDTERQ 211
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 6-122 1.05e-10

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: 64.32  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576   6 AVGRRVCCDGERGTVRYVGPVPPTAGVWLGVEWDHPeRGKHDGSHDGVRYFTCRHPTgGSFVRP---------------- 69
Cdd:COG5244   5 SVNDRVLLGDKFGTVRFIGKTKFKDGIWIGLELDDP-VGKNDGSVNGVRYFHCKKRH-GIFIRPdddsllngnaayekik 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88942576  70 ---QKASFGVDYVTALKQ---RYEVEIEEVTAEEMKI----SSKTVVMVGFENVKKKQSVKNL 122
Cdd:COG5244  83 gglVCESKGMDKDGEIKQenhEDRIHFEESKIRRLEEtieaLKSTEKEEIVELRRENEELDKI 145
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
120-338 3.32e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.79  E-value: 3.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 120 KNLTEVGLRRCEVSA-PGPENEIRNttpfVQSLDLSGNLLSSW-EVLAaiteQLDSLQELHLSHNRLSISSAPSSLSSaf 197
Cdd:COG4886 159 TNLKSLDLSNNQLTDlPEELGNLTN----LKELDLSNNQITDLpEPLG----NLTNLEELDLSGNQLTDLPEPLANLT-- 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 198 sHLRVLSINSCALTWTQVLHCAPmwqQVEELYLADNNITELlRPEHVLQALTVLDLSNNQIaqeTVLEISHLPRLERLNL 277
Cdd:COG4886 229 -NLETLDLSNNQLTDLPELGNLT---NLEELDLSNNQLTDL-PPLANLTNLKTLDLSNNQL---TDLKLKELELLLGLNS 300

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88942576 278 SSTSLSEIKFSDVPAGKKTTLFPALKELLLDDNNISEWRVVNELEKLPSLVYLSCRRNPLL 338
Cdd:COG4886 301 LLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSL 361
LRR_9 pfam14580
Leucine-rich repeat;
251-384 3.09e-08

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 53.23  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576   251 LDLSNNQIAQetvLE-ISHLPRLERLNLSSTSLSEIKfsdvpAGKKTTLfPALKELLLDDNNISEWRVVNELEKLPSLVY 329
Cdd:pfam14580  47 IDFSDNEIRK---LDgFPLLRRLKTLLLNNNRICRIG-----EGLGEAL-PNLTELILTNNNLQELGDLDPLASLKKLTF 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 88942576   330 LSCRRNPLLHKEKnletARQIMIARLGQLELLDMRQILSDERRGAEldycKMFGS 384
Cdd:pfam14580 118 LSLLRNPVTNKPH----YRLYVIYKVPQLRLLDFRKVKQKERQAAE----KMFRS 164
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
199-361 7.98e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 55.09  E-value: 7.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576  199 HLRVLSINSCALTWTQvlhcAPMWQQVEELYLADNNITELlrPEHVLQALTVLDLSNNQIA--QETVLE----------- 265
Cdd:PRK15370 221 NIKTLYANSNQLTSIP----ATLPDTIQEMELSINRITEL--PERLPSALQSLDLFHNKISclPENLPEelrylsvydns 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576  266 ----ISHLPR-LERLNLSSTSLSEIKfSDVPAGKKT-------------TLFPALKELLLDDNNISewrVVNELEKlPSL 327
Cdd:PRK15370 295 irtlPAHLPSgITHLNVQSNSLTALP-ETLPPGLKTleagenaltslpaSLPPELQVLDVSKNQIT---VLPETLP-PTI 369

                        170       180       190
                 ....*....|....*....|....*....|....
gi 88942576  328 VYLSCRRNPLLHKEKNLETARQIMIARLGQLELL 361
Cdd:PRK15370 370 TTLDVSRNALTNLPENLPAALQIMQASRNNLVRL 403
LRR_8 pfam13855
Leucine rich repeat;
223-282 2.11e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.82  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88942576   223 QQVEELYLADNNITELlRPE--HVLQALTVLDLSNNQIaqeTVLE---ISHLPRLERLNLSSTSL 282
Cdd:pfam13855   1 PNLRSLDLSNNRLTSL-DDGafKGLSNLKVLDLSNNLL---TTLSpgaFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 144-338 2.54e-06

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 49.28  E-value: 2.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 144 TTPFVQSLDLSGNLLS--SWEVLAAITeQLDSLQELHLSHNRLSISSAPSSL---SSAFSHLRVLSINSCALTW---TQV 215
Cdd:cd00116  79 KGCGLQELDLSDNALGpdGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAkglKDLPPALEKLVLGRNRLEGascEAL 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 216 LHCAPMWQQVEELYLADNNITE-----LLRPEHVLQALTVLDLSNNQIAQETVLEISHLPR----LERLNLSSTSLSEIK 286
Cdd:cd00116 158 AKALRANRDLKELNLANNGIGDagiraLAEGLKANCNLEVLDLNNNGLTDEGASALAETLAslksLEVLNLGDNNLTDAG 237

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 88942576 287 FSDVPAGKKTTLfPALKELLLDDNNISEWRVVNELEKL---PSLVYLSCRRNPLL 338
Cdd:cd00116 238 AAALASALLSPN-ISLLTLSLSCNDITDDGAKDLAEVLaekESLLELDLRGNKFG 291
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 120-314 7.09e-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: 45.17  E-value: 7.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 120 KNLTEVGLRRCEVSAPGPENEI----RNTTpfVQSLDLSGNLLSSwEVLAAITEQL---DSLQELHLSHNRLSIS--SAP 190
Cdd:COG5238 208 TTVTTLWLKRNPIGDEGAEILAealkGNKS--LTTLDLSNNQIGD-EGVIALAEALknnTTVETLYLSGNQIGAEgaIAL 284

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 191 SSLSSAFSHLRVLSINSCALTWTQVLHCAPMWQQ---VEELYLADNNITE-----LLRPEHVLQALTVLDLSNNQIAQET 262
Cdd:COG5238 285 AKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGnktLHTLNLAYNGIGAqgaiaLAKALQENTTLHSLDLSDNQIGDEG 364

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 88942576 263 VLEISHL----PRLERLNLSSTSLSEIKFSDVPAGKKTTlfpALKELLLDDNNISE 314
Cdd:COG5238 365 AIALAKYlegnTTLRELNLGKNNIGKQGAEALIDALQTN---RLHTLILDGNLIGA 417
LRR_8 pfam13855
Leucine rich repeat;
248-312 2.09e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.43  E-value: 2.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88942576   248 LTVLDLSNNQIaqeTVLE---ISHLPRLERLNLSSTSLSEIK---FSDvpagkkttlFPALKELLLDDNNI 312
Cdd:pfam13855   3 LRSLDLSNNRL---TSLDdgaFKGLSNLKVLDLSNNLLTTLSpgaFSG---------LPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
120-315 1.81e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 120 KNLTEVGLRRCEVSA-PGPENEIRNttpfVQSLDLSGNLLSSwevLAAITEQLDSLQELHLSHNRLSISSAPSSLSsafs 198
Cdd:COG4886 182 TNLKELDLSNNQITDlPEPLGNLTN----LEELDLSGNQLTD---LPEPLANLTNLETLDLSNNQLTDLPELGNLT---- 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88942576 199 HLRVLSINSCALTWtqvLHCAPMWQQVEELYLADNNITElLRPEHVLQALTVLDLSNNQIAQETVLEISHLPRLERLNLS 278
Cdd:COG4886 251 NLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLTD-LKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 88942576 279 STSLSEIKFSDVPAGKKTTLFPALKELLLDDNNISEW 315
Cdd:COG4886 327 LLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLL 363
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 248-286 2.55e-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: 35.68  E-value: 2.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 88942576   248 LTVLDLSNNQIaqETVLEISHLPRLERLNLSS----TSLSEIK 286
Cdd:pfam12799   3 LEVLDLSNNQI--TDIPPLAKLPNLETLDLSGnnkiTDLSDLA 43
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 223-256 3.67e-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: 35.30  E-value: 3.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 88942576   223 QQVEELYLADNNITElLRPEHVLQALTVLDLSNN 256
Cdd:pfam12799   1 PNLEVLDLSNNQITD-IPPLAKLPNLETLDLSGN 33
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 300-345 7.61e-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: 34.53  E-value: 7.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 88942576   300 PALKELLLDDNNISEwrvVNELEKLPSLVYLSCRRNPLLHKEKNLE 345
Cdd:pfam12799   1 PNLEVLDLSNNQITD---IPPLAKLPNLETLDLSGNNKITDLSDLA 43
 
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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