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Conserved domains on  [gi|443287660|ref|NP_001263208|]
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ubiquitin carboxyl-terminal hydrolase CYLD isoform c [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 407-762 6.17e-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: 256.30  E-value: 6.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 407 GIQGHYN-SCYLDSTLFCLFAfssaldtvllrpkekndieyysetqellrteivnplriygyvcatkimklrkilekvea 485
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 486 asgftsEEKDPEEFLNILFHDILR--VEPLLKIRSAGQKVQD------CNFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 557
Cdd:cd02670   22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 558 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGKIKQFCKT 633
Cdd:cd02670   95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 634 CSTQVHLHPRRlnhsyhpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 703
Cdd:cd02670  170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 443287660 704 SMADRDGGQNGFNIPqvtpcpevgeylkmsledlhsldsrriqgcARRLLCDAYMCMYQ 762
Cdd:cd02670  213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CYLD_phos_site super family cl24982
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 304-375 2.04e-45

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.


The actual alignment was detected with superfamily member pfam16607:

Pssm-ID: 465194  Cd Length: 157  Bit Score: 159.73  E-value: 2.04e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287660  304 PDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQ-QSKSKNPWYIDE 375
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQpQPKSKNTWYIDE 73
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 127-203 1.37e-17

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: 77.63  E-value: 1.37e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 443287660   127 VGSPVKVqlrsGEEKFPGVVRFRGPLLaerTVSGIFFGVELLEEGRGqgFTDGVYQGKQLFQCDEDCGVFVALDKLE 203
Cdd:smart01052   1 VGDRVEV----GGGGRRGTVRYVGPTP---FAPGVWVGVELDEPLRG--KNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 232-286 4.43e-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: 56.05  E-value: 4.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 443287660   232 INSRVslKVGESTESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 286
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
 
Name Accession Description Interval E-value
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 407-762 6.17e-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: 256.30  E-value: 6.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 407 GIQGHYN-SCYLDSTLFCLFAfssaldtvllrpkekndieyysetqellrteivnplriygyvcatkimklrkilekvea 485
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 486 asgftsEEKDPEEFLNILFHDILR--VEPLLKIRSAGQKVQD------CNFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 557
Cdd:cd02670   22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 558 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGKIKQFCKT 633
Cdd:cd02670   95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 634 CSTQVHLHPRRlnhsyhpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 703
Cdd:cd02670  170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 443287660 704 SMADRDGGQNGFNIPqvtpcpevgeylkmsledlhsldsrriqgcARRLLCDAYMCMYQ 762
Cdd:cd02670  213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 304-375 2.04e-45

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: 159.73  E-value: 2.04e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287660  304 PDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQ-QSKSKNPWYIDE 375
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQpQPKSKNTWYIDE 73
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 127-203 1.37e-17

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: 77.63  E-value: 1.37e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 443287660   127 VGSPVKVqlrsGEEKFPGVVRFRGPLLaerTVSGIFFGVELLEEGRGqgFTDGVYQGKQLFQCDEDCGVFVALDKLE 203
Cdd:smart01052   1 VGDRVEV----GGGGRRGTVRYVGPTP---FAPGVWVGVELDEPLRG--KNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 127-202 1.62e-12

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: 62.81  E-value: 1.62e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287660  127 VGSPVKVqlrsgEEKFPGVVRFRGPLlaeRTVSGIFFGVELlEEGRGQgfTDGVYQGKQLFQCDEDCGVFVALDKL 202
Cdd:pfam01302   1 VGDRVEV-----PGGRRGTVRYVGPV---PFAPGVWVGVEL-DEPVGK--NDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 232-286 4.43e-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: 56.05  E-value: 4.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 443287660   232 INSRVslKVGESTESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 286
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 232-284 9.56e-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: 43.93  E-value: 9.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 443287660  232 INSRVSLkvgESTESGTVIFCDVLPGKEslGYFVGVDMDNPIGNWDGRFDGVQ 284
Cdd:pfam01302   1 VGDRVEV---PGGRRGTVRYVGPVPFAP--GVWVGVELDEPVGKNDGSVKGVR 48
 
Name Accession Description Interval E-value
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 407-762 6.17e-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: 256.30  E-value: 6.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 407 GIQGHYN-SCYLDSTLFCLFAfssaldtvllrpkekndieyysetqellrteivnplriygyvcatkimklrkilekvea 485
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 486 asgftsEEKDPEEFLNILFHDILR--VEPLLKIRSAGQKVQD------CNFYQIFMEKNEKVGVPTIQQLLEWSFINSNl 557
Cdd:cd02670   22 ------EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQDddklvnERLLQIPVPDDDDGGGITLEQCLEQYFNNSV- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 558 kFAEAPSCLIIQMPRFGK----DFKLFKKIFPSLELNITDLLEDTPRQCRICGglamYECRECYDDPDISAGKIKQFCKT 633
Cdd:cd02670   95 -FAKAPSCLIICLKRYGKtegkAQKMFKKILIPDEIDIPDFVADDPRACSKCQ----LECRVCYDDKDFSPTCGKFKLSL 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 634 CSTQVHLHPRRlnhsyhpvslpkdlpdwdwrhgcipcqkmelfavlciETSHYVAFVKYGKD----------DSAWLFFD 703
Cdd:cd02670  170 CSAVCHRGTSL-------------------------------------ETGHYVAFVRYGSYsltetdneayNAQWVFFD 212

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 443287660 704 SMADRDGGQNGFNIPqvtpcpevgeylkmsledlhsldsrriqgcARRLLCDAYMCMYQ 762
Cdd:cd02670  213 DMADRDGVSNGFNIP------------------------------AARLLEDPYMLFYQ 241
CYLD_phos_site pfam16607
Phosphorylation region of CYLD, unstructured; CYLD_phos_site is a natively unstructured region ...
 304-375 2.04e-45

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: 159.73  E-value: 2.04e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287660  304 PDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQ-QSKSKNPWYIDE 375
Cdd:pfam16607   1 PESVSQERRPPKLAFASRGGGDKGSSSHNKPKATGSTSDPGNRNRSEFFYTLNGSSVDSQpQPKSKNTWYIDE 73
Bbox1_CYLD cd19816
B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; ...
 599-655 5.32e-23

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: 92.53  E-value: 5.32e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443287660 599 PRQCRICGGLAMYECRECYDDPDISaGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLP 655
Cdd:cd19816    1 PRECIICGGLAEYECRDCYLDPGIG-GKIKAFCKKCNKQTHLHPKRQNHKPRPLSVP 56
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 127-203 1.37e-17

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: 77.63  E-value: 1.37e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 443287660   127 VGSPVKVqlrsGEEKFPGVVRFRGPLLaerTVSGIFFGVELLEEGRGqgFTDGVYQGKQLFQCDEDCGVFVALDKLE 203
Cdd:smart01052   1 VGDRVEV----GGGGRRGTVRYVGPTP---FAPGVWVGVELDEPLRG--KNDGSVKGVRYFECPPKHGIFVRPSKVE 68
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 127-202 1.62e-12

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: 62.81  E-value: 1.62e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287660  127 VGSPVKVqlrsgEEKFPGVVRFRGPLlaeRTVSGIFFGVELlEEGRGQgfTDGVYQGKQLFQCDEDCGVFVALDKL 202
Cdd:pfam01302   1 VGDRVEV-----PGGRRGTVRYVGPV---PFAPGVWVGVEL-DEPVGK--NDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 232-286 4.43e-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: 56.05  E-value: 4.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 443287660   232 INSRVslKVGESTESGTVIFCDVLPGKEslGYFVGVDMDNP-IGNWDGRFDGVQLC 286
Cdd:smart01052   1 VGDRV--EVGGGGRRGTVRYVGPTPFAP--GVWVGVELDEPlRGKNDGSVKGVRYF 52
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 407-762 2.02e-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: 59.03  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 407 GIQGHYNSCYLDSTLFCLFAfssaldtvllrpkEKNDieyyseTQELLRteivnplriygyvcatkimklrKILEKVEAA 486
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFS-------------EQQD------AHEFLL----------------------FLLDKLHEE 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 487 SGFTSEEKDPEEFLNILFHDILRVEplLKIR-------SAGQKVQDCNFYQIFMEKNEKvGVPTIQQLLEWSFINSNL-- 557
Cdd:cd02257   40 LKKSSKRTSDSSSLKSLIHDLFGGK--LESTivclecgHESVSTEPELFLSLPLPVKGL-PQVSLEDCLEKFFKEEILeg 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 558 ------------------KFAEAPSCLIIQMPRFGKDF-----KLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYecr 614
Cdd:cd02257  117 dncykcekkkkqeatkrlKIKKLPPVLIIHLKRFSFNEdgtkeKLNTKVSFPLELDLSPYLSEGEKDSDSDNGSYKY--- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287660 615 ecyddpdisagkikqfcktcstqvhlhprrlnhsyhpvslpkdlpdwdwrhgcipcqkmELFAVLC-----IETSHYVAF 689
Cdd:cd02257  194 -----------------------------------------------------------ELVAVVVhsgtsADSGHYVAY 214

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287660 690 VKYGKDDSaWLFFDSMadrdggqngfnipQVTPCPEvgeylkmslEDLHSLdsrriqgcaRRLLCDAYMCMYQ 762
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 ...
 232-284 9.56e-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: 43.93  E-value: 9.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 443287660  232 INSRVSLkvgESTESGTVIFCDVLPGKEslGYFVGVDMDNPIGNWDGRFDGVQ 284
Cdd:pfam01302   1 VGDRVEV---PGGRRGTVRYVGPVPFAP--GVWVGVELDEPVGKNDGSVKGVR 48
Bbox1_DUF2009 cd20208
B-box-type 1 zinc finger found in DUF2009 domain-containing proteins and similar proteins; ...
 601-652 1.78e-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: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 443287660 601 QCRICG-GLAMYECRECYDDpdisagkikqFCKTCSTQVHLHPRRLNHSYHPV 652
Cdd:cd20208    1 MCIECEdQPAEVRCEECGDE----------FCEVCFQSQHRKGKRRLHSFRPV 43
Bbox1_HOIP cd19815
B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, ...
 601-647 4.56e-03

B-box-type 1 zinc finger found in HOIL-1-interacting protein (HOIP) and similar proteins; HOIP, also termed RING finger protein 31 (RNF31), or zinc in-between-RING-finger ubiquitin-associated domain protein, together with HOIL-1 and SHARPIN, forms the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis. It also interacts with the atypical mammalian orphan receptor DAX-1, trigger DAX-1 ubiquitination and stabilization, and participate in repressing steroidogenic gene expression. HOIP contains a B-box motif that 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: 380873  Cd Length: 43  Bit Score: 35.39  E-value: 4.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 443287660 601 QCRICGGL-AMYECRECYDdpdisagkikQFCKTCSTQVHLHPRRLNH 647
Cdd:cd19815    1 LCDLCGEAaASVFCASCED----------KLCLSCDDLYHKHPARRSH 38
 
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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