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Conserved domains on  [gi|392896298|ref|NP_001255047|]
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ubiquitinyl hydrolase 1 [Caenorhabditis elegans]

Protein Classification

CAP-Gly domain-containing protein; TBCE family protein( domain architecture ID 10660430)

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
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
456-811 4.93e-69

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: 228.18  E-value: 4.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 456 GIQGYCN-SCYLDATLYAMFVqttcfdflleksikgsetaqqfqkilaheivfplrkvhyvradhvmklrkllaelmphv 534
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 535 tgltnEEKDPEEILGFIFSKVFH--AEPFIKLIGQNHAKD------SQYLVPIVVDDWL-GGAATSQHLLERHMRSAQvt 605
Cdd:cd02670   22 -----EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQdddklvNERLLQIPVPDDDdGGGITLEQCLEQYFNNSV-- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 606 FAKAPPVLIMQLPRYGQ-----QKVFDKILPLETIDITPFVAGAVPACSKCQacsevycptcfLTRRVFYSEVIFCRKCF 680
Cdd:cd02670   95 FAKAPSCLIICLKRYGKtegkaQKMFKKILIPDEIDIPDFVADDPRACSKCQ-----------LECRVCYDDKDFSPTCG 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 681 HHTHLLPEIEDHKSRDLyppgkpqkkphshkmvlsavlciETSHYVAYVRTSS------------NQWVFFDSMADREGL 748
Cdd:cd02670  164 KFKLSLCSAVCHRGTSL-----------------------ETGHYVAFVRYGSysltetdneaynAQWVFFDDMADRDGV 220
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896298 749 SDGFNVPvvrecgnmsdwlslqgwnrlkdadecgqikamfgkqssldplVGRLLSDSYICFYE 811
Cdd:cd02670  221 SNGFNIP------------------------------------------AARLLEDPYMLFYQ 241
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
150-212 2.06e-12

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: 62.99  E-value: 2.06e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896298   150 IGDQCIWNNNGaeERGIIKYIGFLKGHKTLYAGVEFKN-TIGAGTGVFNREQLFLAKDGHAGFV 212
Cdd:smart01052   1 VGDRVEVGGGG--RRGTVRYVGPTPFAPGVWVGVELDEpLRGKNDGSVKGVRYFECPPKHGIFV 62
 
Name Accession Description Interval E-value
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
456-811 4.93e-69

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: 228.18  E-value: 4.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 456 GIQGYCN-SCYLDATLYAMFVqttcfdflleksikgsetaqqfqkilaheivfplrkvhyvradhvmklrkllaelmphv 534
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 535 tgltnEEKDPEEILGFIFSKVFH--AEPFIKLIGQNHAKD------SQYLVPIVVDDWL-GGAATSQHLLERHMRSAQvt 605
Cdd:cd02670   22 -----EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQdddklvNERLLQIPVPDDDdGGGITLEQCLEQYFNNSV-- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 606 FAKAPPVLIMQLPRYGQ-----QKVFDKILPLETIDITPFVAGAVPACSKCQacsevycptcfLTRRVFYSEVIFCRKCF 680
Cdd:cd02670   95 FAKAPSCLIICLKRYGKtegkaQKMFKKILIPDEIDIPDFVADDPRACSKCQ-----------LECRVCYDDKDFSPTCG 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 681 HHTHLLPEIEDHKSRDLyppgkpqkkphshkmvlsavlciETSHYVAYVRTSS------------NQWVFFDSMADREGL 748
Cdd:cd02670  164 KFKLSLCSAVCHRGTSL-----------------------ETGHYVAFVRYGSysltetdneaynAQWVFFDDMADRDGV 220
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896298 749 SDGFNVPvvrecgnmsdwlslqgwnrlkdadecgqikamfgkqssldplVGRLLSDSYICFYE 811
Cdd:cd02670  221 SNGFNIP------------------------------------------AARLLEDPYMLFYQ 241
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
150-212 2.06e-12

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: 62.99  E-value: 2.06e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896298   150 IGDQCIWNNNGaeERGIIKYIGFLKGHKTLYAGVEFKN-TIGAGTGVFNREQLFLAKDGHAGFV 212
Cdd:smart01052   1 VGDRVEVGGGG--RRGTVRYVGPTPFAPGVWVGVELDEpLRGKNDGSVKGVRYFECPPKHGIFV 62
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
150-212 1.23e-07

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: 49.32  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896298  150 IGDQCiwnNNGAEERGIIKYIGFLKGHKTLYAGVEFKNTIGAGTGVFNREQLFLAKDGHAGFV 212
Cdd:pfam01302   1 VGDRV---EVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFV 60
 
Name Accession Description Interval E-value
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
456-811 4.93e-69

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: 228.18  E-value: 4.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 456 GIQGYCN-SCYLDATLYAMFVqttcfdflleksikgsetaqqfqkilaheivfplrkvhyvradhvmklrkllaelmphv 534
Cdd:cd02670    1 GAQNHCNvSCYLDALLFAMFA----------------------------------------------------------- 21
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 535 tgltnEEKDPEEILGFIFSKVFH--AEPFIKLIGQNHAKD------SQYLVPIVVDDWL-GGAATSQHLLERHMRSAQvt 605
Cdd:cd02670   22 -----EQQDPEEFFNFITDKLLMplLEPKVDIIHGGKKDQdddklvNERLLQIPVPDDDdGGGITLEQCLEQYFNNSV-- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 606 FAKAPPVLIMQLPRYGQ-----QKVFDKILPLETIDITPFVAGAVPACSKCQacsevycptcfLTRRVFYSEVIFCRKCF 680
Cdd:cd02670   95 FAKAPSCLIICLKRYGKtegkaQKMFKKILIPDEIDIPDFVADDPRACSKCQ-----------LECRVCYDDKDFSPTCG 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 681 HHTHLLPEIEDHKSRDLyppgkpqkkphshkmvlsavlciETSHYVAYVRTSS------------NQWVFFDSMADREGL 748
Cdd:cd02670  164 KFKLSLCSAVCHRGTSL-----------------------ETGHYVAFVRYGSysltetdneaynAQWVFFDDMADRDGV 220
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896298 749 SDGFNVPvvrecgnmsdwlslqgwnrlkdadecgqikamfgkqssldplVGRLLSDSYICFYE 811
Cdd:cd02670  221 SNGFNIP------------------------------------------AARLLEDPYMLFYQ 241
Bbox1_CYLD cd19816
B-box-type 1 zinc finger found in tumor suppressor cylindromatosis (CYLD) and similar proteins; ...
646-700 8.19e-18

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: 77.90  E-value: 8.19e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392896298 646 PACSKCQACSEVYCPTCFLTRRVFYSEVIFCRKCFHHTHLLPEIEDHKSRDLYPP 700
Cdd:cd19816    2 RECIICGGLAEYECRDCYLDPGIGGKIKAFCKKCNKQTHLHPKRQNHKPRPLSVP 56
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
150-212 2.06e-12

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: 62.99  E-value: 2.06e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896298   150 IGDQCIWNNNGaeERGIIKYIGFLKGHKTLYAGVEFKN-TIGAGTGVFNREQLFLAKDGHAGFV 212
Cdd:smart01052   1 VGDRVEVGGGG--RRGTVRYVGPTPFAPGVWVGVELDEpLRGKNDGSVKGVRYFECPPKHGIFV 62
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
150-212 1.23e-07

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: 49.32  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896298  150 IGDQCiwnNNGAEERGIIKYIGFLKGHKTLYAGVEFKNTIGAGTGVFNREQLFLAKDGHAGFV 212
Cdd:pfam01302   1 VGDRV---EVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFV 60
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
456-740 4.97e-06

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: 49.02  E-value: 4.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 456 GIQGYCNSCYLDATLYAMFVQ----TTCFDFL---LEKSIKGSETAQQFQKILAHEIVFPLRkvhyvradhvmklRKLLA 528
Cdd:cd02257    1 GLNNLGNTCYLNSVLQALFSEqqdaHEFLLFLldkLHEELKKSSKRTSDSSSLKSLIHDLFG-------------GKLES 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 529 ELMPHVTGLTNEEKDPEEILGF-IFSKVFHAEPFIKLIgqnhakdSQYLVPIVVDDWLGGAATSQHLLERHMRSaqvTFA 607
Cdd:cd02257   68 TIVCLECGHESVSTEPELFLSLpLPVKGLPQVSLEDCL-------EKFFKEEILEGDNCYKCEKKKKQEATKRL---KIK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896298 608 KAPPVLIMQLPRYGQ------QKVFDKILPLETIDITPFVagavpacskcqacsevycptcfltrrvfysevifcrkcfh 681
Cdd:cd02257  138 KLPPVLIIHLKRFSFnedgtkEKLNTKVSFPLELDLSPYL---------------------------------------- 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896298 682 hTHLLPEIEDHKSRDLYppgkpqkkphshkmVLSAVLC-----IETSHYVAYVR-TSSNQWVFFD 740
Cdd:cd02257  178 -SEGEKDSDSDNGSYKY--------------ELVAVVVhsgtsADSGHYVAYVKdPSDGKWYKFN 227
 
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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