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Conserved domains on  [gi|1907191448|ref|XP_036010225|]
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ubiquitin carboxyl-terminal hydrolase CYLD isoform X5 [Mus musculus]

Protein Classification

CAP-Gly domain-containing protein; TBCE family protein( domain architecture ID 11279563)

CAP (cytoskeleton-associated protein)-Gly domain-containing protein similar to Schizosaccharomyces pombe Tip elongation protein 1 that has a role in stabilizing and targeting the growing tips of the microtubules along the long axis of the cell, directing them to the ends of the cell| TBCE (tubulin-specific chaperone E) family protein similar to Homo sapiens tubulin-specific chaperone E, a tubulin-folding protein involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 85-240 4.56e-96

Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction.


:

Pssm-ID: 465194  Cd Length: 157  Bit Score: 294.17  E-value: 4.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448  85 SDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQ-QSKSKNPWYIDEVAEDPAK 163
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQpQPKSKNTWYIDEVAEDPAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907191448 164 SLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPIS 240
Cdd:pfam16607  81 SLTDTSPGFGHSSPPLQPPPTNSLSSENRFHSLPFSLTKMPSSNGSIGHSPLSLSVQSVMGELNTGPVQESPPSAAP 157
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-725 1.65e-80

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


:

Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 256.68  E-value: 1.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 370 GIQGHYN-SCYLDSTLFCLFAfssaldtvllrpkekndieyysetqellrteivnplriygyvcatkimklrkilekvea 448
Cdd:cd02670     1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 449 asgftsEEKDPEEFLNILFHDILR--VEPLLKIRSAGQKVQD------CNFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 520
Cdd:cd02670    22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 521 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGKIKQFCKT 596
Cdd:cd02670    95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 597 CSTQVHLHPRRlnhsyhpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 666
Cdd:cd02670   170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191448 667 SMADRDGGQNGFNIPqvtpcpevgeylkmsledlhsldsrriqgcARRLLCDAYMCMYQ 725
Cdd:cd02670   213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 249-317 3.16e-22

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: 90.72  E-value: 3.16e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191448  249 VGSLAEVKENPpFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCR 317
Cdd:smart01052   1 VGDRVEVGGGG-RRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-64 1.51e-10

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: 57.21  E-value: 1.51e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907191448   10 INSRVslKVGESTESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 64
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
 
Name Accession Description Interval E-value
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 85-240 4.56e-96

Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction.


Pssm-ID: 465194  Cd Length: 157  Bit Score: 294.17  E-value: 4.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448  85 SDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQ-QSKSKNPWYIDEVAEDPAK 163
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQpQPKSKNTWYIDEVAEDPAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907191448 164 SLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPIS 240
Cdd:pfam16607  81 SLTDTSPGFGHSSPPLQPPPTNSLSSENRFHSLPFSLTKMPSSNGSIGHSPLSLSVQSVMGELNTGPVQESPPSAAP 157
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-725 1.65e-80

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 256.68  E-value: 1.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 370 GIQGHYN-SCYLDSTLFCLFAfssaldtvllrpkekndieyysetqellrteivnplriygyvcatkimklrkilekvea 448
Cdd:cd02670     1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 449 asgftsEEKDPEEFLNILFHDILR--VEPLLKIRSAGQKVQD------CNFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 520
Cdd:cd02670    22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 521 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGKIKQFCKT 596
Cdd:cd02670    95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 597 CSTQVHLHPRRlnhsyhpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 666
Cdd:cd02670   170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191448 667 SMADRDGGQNGFNIPqvtpcpevgeylkmsledlhsldsrriqgcARRLLCDAYMCMYQ 725
Cdd:cd02670   213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 249-317 3.16e-22

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: 90.72  E-value: 3.16e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191448  249 VGSLAEVKENPpFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCR 317
Cdd:smart01052   1 VGDRVEVGGGG-RRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 255-316 9.57e-17

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: 74.75  E-value: 9.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907191448 255 VKENPPFYGVIRWIGQPPGLSDVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSC 316
Cdd:pfam01302   5 VEVPGGRRGTVRYVGPVPFAPGVWVGVEL-DEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-64 1.51e-10

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: 57.21  E-value: 1.51e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907191448   10 INSRVslKVGESTESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 64
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-62 3.44e-06

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: 45.09  E-value: 3.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907191448  10 INSRVSLkvgESTESGTVIFCDVLPGKEslGYFVGVDMDNPIGNWDGRFDGVQ 62
Cdd:pfam01302   1 VGDRVEV---PGGRRGTVRYVGPVPFAP--GVWVGVELDEPVGKNDGSVKGVR 48
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 262-363 1.13e-04

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: 45.45  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 262 YGVIRWIGQPPGLSDVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFG 341
Cdd:COG5244    16 FGTVRFIGKTKFKDGIWIGLEL-DDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGNAAYEKIKGGLVCESKGMDK 94

                          90       100
                  ....*....|....*....|..
gi 1907191448 342 gyLSEVVEENTPPKMEKEGLEI 363
Cdd:COG5244    95 --DGEIKQENHEDRIHFEESKI 114
 
Name Accession Description Interval E-value
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 85-240 4.56e-96

Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region on a subset of tumour-suppressor and de-ubiquitinating enzyme CYLD proteins in eukaryotes. It lies between the second pair of CAP_GLY domains, pfam01302, on these proteins. This region of CYLD, being unstructured, carries a number of serine residues which, in response to cellular stimuli, become phosphorylated. This transient phosphorylation-state induces ubiquitination of TRAF2, a ubiquitin ligase that catalyzes both self-ubiquitination and the ubiquitination of specific target molecules involved in signal transduction.


Pssm-ID: 465194  Cd Length: 157  Bit Score: 294.17  E-value: 4.56e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448  85 SDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQ-QSKSKNPWYIDEVAEDPAK 163
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQpQPKSKNTWYIDEVAEDPAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907191448 164 SLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPIS 240
Cdd:pfam16607  81 SLTDTSPGFGHSSPPLQPPPTNSLSSENRFHSLPFSLTKMPSSNGSIGHSPLSLSVQSVMGELNTGPVQESPPSAAP 157
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 370-725 1.65e-80

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 256.68  E-value: 1.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 370 GIQGHYN-SCYLDSTLFCLFAfssaldtvllrpkekndieyysetqellrteivnplriygyvcatkimklrkilekvea 448
Cdd:cd02670     1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 449 asgftsEEKDPEEFLNILFHDILR--VEPLLKIRSAGQKVQD------CNFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 520
Cdd:cd02670    22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 521 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGKIKQFCKT 596
Cdd:cd02670    95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 597 CSTQVHLHPRRlnhsyhpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 666
Cdd:cd02670   170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191448 667 SMADRDGGQNGFNIPqvtpcpevgeylkmsledlhsldsrriqgcARRLLCDAYMCMYQ 725
Cdd:cd02670   213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
Bbox1_CYLD cd19816
B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; ...
 562-618 1.26e-22

B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; CYLD, also termed ubiquitin carboxyl-terminal hydrolase CYLD, or deubiquitinating enzyme CYLD, or ubiquitin thioesterase CYLD, or ubiquitin-specific-processing protease CYLD, is a microtubule-associated deubiquitinase that specifically cleaves Lys-63-linked polyubiquitin chains. It plays a pivotal role in a wide range of cellular activities, including innate immunity, cell division, and ciliogenesis. CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Structural characterization reveals a small zinc-binding B-box inserted within the ubiquitin specific protease (USP) domain of CYLD. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs) and is responsible for its intermolecular interaction and cytoplasmic localization. The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380874  Cd Length: 56  Bit Score: 91.38  E-value: 1.26e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907191448 562 PRQCRICGGLAMYECRECYDDPDISaGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLP 618
Cdd:cd19816     1 PRECIICGGLAEYECRDCYLDPGIG-GKIKAFCKKCNKQTHLHPKRQNHKPRPLSVP 56
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 249-317 3.16e-22

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: 90.72  E-value: 3.16e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191448  249 VGSLAEVKENPpFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCR 317
Cdd:smart01052   1 VGDRVEVGGGG-RRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 255-316 9.57e-17

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: 74.75  E-value: 9.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907191448 255 VKENPPFYGVIRWIGQPPGLSDVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSC 316
Cdd:pfam01302   5 VEVPGGRRGTVRYVGPVPFAPGVWVGVEL-DEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 10-64 1.51e-10

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: 57.21  E-value: 1.51e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907191448   10 INSRVslKVGESTESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 64
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 370-725 1.14e-09

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 59.80  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 370 GIQGHYNSCYLDSTLFCLFAfssaldtvllrpkEKNDieyyseTQELLRteivnplriygyvcatkimklrKILEKVEAA 449
Cdd:cd02257     1 GLNNLGNTCYLNSVLQALFS-------------EQQD------AHEFLL----------------------FLLDKLHEE 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 450 SGFTSEEKDPEEFLNILFHDILRVEplLKIR-------SAGQKVQDCNFYQIFMEKNEKvGVPTIQQLLEWSFINSNL-- 520
Cdd:cd02257    40 LKKSSKRTSDSSSLKSLIHDLFGGK--LESTivclecgHESVSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILeg 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 521 ------------------KFAEAPSCLIIQMPRFGKDF-----KLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYecr 577
Cdd:cd02257   117 dncykcekkkkqeatkrlKIKKLPPVLIIHLKRFSFNEdgtkeKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKY--- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 578 ecyddpdisagkikqfcktcstqvhlhprrlnhsyhpvslpkdlpdwdwrhgcipcqkmELFAVLC-----IETSHYVAF 652
Cdd:cd02257   194 -----------------------------------------------------------ELVAVVVhsgtsADSGHYVAY 214

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907191448 653 VKYGKDDSaWLFFDSMadrdggqngfnipQVTPCPEvgeylkmslEDLHSLdsrriqgcaRRLLCDAYMCMYQ 725
Cdd:cd02257   215 VKDPSDGK-WYKFNDD-------------KVTEVSE---------EEVLEF---------GSLSSSAYILFYE 255
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 10-62 3.44e-06

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: 45.09  E-value: 3.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907191448  10 INSRVSLkvgESTESGTVIFCDVLPGKEslGYFVGVDMDNPIGNWDGRFDGVQ 62
Cdd:pfam01302   1 VGDRVEV---PGGRRGTVRYVGPVPFAP--GVWVGVELDEPVGKNDGSVKGVR 48
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 262-363 1.13e-04

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: 45.45  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191448 262 YGVIRWIGQPPGLSDVLAGLELeDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFG 341
Cdd:COG5244    16 FGTVRFIGKTKFKDGIWIGLEL-DDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGNAAYEKIKGGLVCESKGMDK 94

                          90       100
                  ....*....|....*....|..
gi 1907191448 342 gyLSEVVEENTPPKMEKEGLEI 363
Cdd:COG5244    95 --DGEIKQENHEDRIHFEESKI 114
Bbox1_DUF2009 cd20208
B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; ...
 564-615 1.69e-03

B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; This group is composed of uncharacterized proteins containing a zinc finger B-box domain and a DUF2009 domain, and similar zinc finger B-box domain-containing proteins. The B-box motif shows high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterized by a C6H2 zinc-binding consensus motif.


Pssm-ID: 380909 [Multi-domain]  Cd Length: 43  Bit Score: 36.58  E-value: 1.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907191448 564 QCRICG-GLAMYECRECYDDpdisagkikqFCKTCSTQVHLHPRRLNHSYHPV 615
Cdd:cd20208     1 MCIECEdQPAEVRCEECGDE----------FCEVCFQSQHRKGKRRLHSFRPV 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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