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Conserved domains on  [gi|13543681|gb|AAH05991|]
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USP45 protein [Homo sapiens]

Protein Classification

UBP-type zinc finger domain-containing protein( domain architecture ID 10489716)

UBP-type zinc finger (zf-UBP) domain-containing protein similar to UBP domain region of histone deacetylases (HDACs) which are a class of enzymes that remove acetyl groups (O=C-CH3) from an e-N-acetyl lysine amino acid on a histone, allowing the histones to wrap the DNA more tightly

CATH:  3.30.40.10
Gene Ontology:  GO:0008270

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 4.13e-15

Zn-finger in ubiquitin-hydrolases and other protein;


:

Pssm-ID: 460464  Cd Length: 63  Bit Score: 68.44  E-value: 4.13e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543681    62 CSECLeerrfydgqlvLTSDIWLCLKCGFQGCGKNSESqHSLKHFKSSRtepHCIIINLSTWIIWCYECDE 132
Cdd:pfam02148   1 CSLCG-----------NTSNLWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
Peptidase_C19 super family cl02553
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
191-220 6.82e-10

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.


The actual alignment was detected with superfamily member cd02667:

Pssm-ID: 470612 [Multi-domain]  Cd Length: 279  Bit Score: 58.55  E-value: 6.82e-10
                        10        20        30
                ....*....|....*....|....*....|
gi 13543681 191 GITNLGNTCFFNAVMQNLAQTYTLTDLMNE 220
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE 30
 
Name Accession Description Interval E-value
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 4.13e-15

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 68.44  E-value: 4.13e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543681    62 CSECLeerrfydgqlvLTSDIWLCLKCGFQGCGKNSESqHSLKHFKSSRtepHCIIINLSTWIIWCYECDE 132
Cdd:pfam02148   1 CSLCG-----------NTSNLWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-220 6.82e-10

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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 58.55  E-value: 6.82e-10
                        10        20        30
                ....*....|....*....|....*....|
gi 13543681 191 GITNLGNTCFFNAVMQNLAQTYTLTDLMNE 220
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE 30
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 4.38e-06

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 43.12  E-value: 4.38e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543681     62 CSECLeerrfydgqlvLTSDIWLCLKCGFQGCGkNSESQHSLKHFKSSRtepHCIIINLST 122
Cdd:smart00290   2 CSVCG-----------TIENLWLCLTCGQVGCG-RYQNGHALEHFEETG---HPLVVKLGT 47
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
190-279 6.86e-05

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 43.59  E-value: 6.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543681   190 RGITNLGNTCFFNAVMQNLAQTYTLTDLMNEIKESSTKLKIFPSSDsqldpLVVELSRpgpltsalfLFLHSMKETEKGP 269
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-----LLCALRD---------LFKALQKNSKSSS 66
                          90
                  ....*....|
gi 13543681   270 LSPKVLFNQL 279
Cdd:pfam00443  67 VSPKMFKKSL 76
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
191-230 1.31e-03

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 39.79  E-value: 1.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 13543681 191 GITNLGNTCFFNAVMQNLA------------QTYTLTDLMNEIKESSTKLKI 230
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlylpkldellddLSKELKVLKNVIRKPEPDLNQ 52
 
Name Accession Description Interval E-value
zf-UBP pfam02148
Zn-finger in ubiquitin-hydrolases and other protein;
62-132 4.13e-15

Zn-finger in ubiquitin-hydrolases and other protein;


Pssm-ID: 460464  Cd Length: 63  Bit Score: 68.44  E-value: 4.13e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543681    62 CSECLeerrfydgqlvLTSDIWLCLKCGFQGCGKNSESqHSLKHFKSSRtepHCIIINLSTWIIWCYECDE 132
Cdd:pfam02148   1 CSLCG-----------NTSNLWLCLTCGHVGCGRYQNS-HALEHYEETG---HPLAVNLSTLTVYCYPCDD 56
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-220 6.82e-10

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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 58.55  E-value: 6.82e-10
                        10        20        30
                ....*....|....*....|....*....|
gi 13543681 191 GITNLGNTCFFNAVMQNLAQTYTLTDLMNE 220
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE 30
ZnF_UBP smart00290
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;
62-122 4.38e-06

Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger;


Pssm-ID: 197632  Cd Length: 50  Bit Score: 43.12  E-value: 4.38e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543681     62 CSECLeerrfydgqlvLTSDIWLCLKCGFQGCGkNSESQHSLKHFKSSRtepHCIIINLST 122
Cdd:smart00290   2 CSVCG-----------TIENLWLCLTCGQVGCG-RYQNGHALEHFEETG---HPLVVKLGT 47
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
190-279 6.86e-05

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 43.59  E-value: 6.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543681   190 RGITNLGNTCFFNAVMQNLAQTYTLTDLMNEIKESSTKLKIFPSSDsqldpLVVELSRpgpltsalfLFLHSMKETEKGP 269
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN-----LLCALRD---------LFKALQKNSKSSS 66
                          90
                  ....*....|
gi 13543681   270 LSPKVLFNQL 279
Cdd:pfam00443  67 VSPKMFKKSL 76
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-279 8.07e-05

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 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: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 43.47  E-value: 8.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13543681 191 GITNLGNTCFFNAVMQNLaqtYTLTDLMNEIKESSTKLKifpSSDSQLDPLVVELSRpgpltsaLFlflHSMKETEKgPL 270
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCL---RSVPELRDALKNYNPARR---GANQSSDNLTNALRD-------LF---DTMDKKQE-PV 63

                ....*....
gi 13543681 271 SPKVLFNQL 279
Cdd:cd02657  64 PPIEFLQLL 72
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
191-245 9.74e-05

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: 42.86  E-value: 9.74e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13543681 191 GITNLGNTCFFNAVMQNL------AQTYtLTDLMNEIKESSTKLKIFPSSDSQLDPLVVEL 245
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALfseqqdAHEF-LLFLLDKLHEELKKSSKRTSDSSSLKSLIHDL 60
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
191-230 1.31e-03

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 39.79  E-value: 1.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 13543681 191 GITNLGNTCFFNAVMQNLA------------QTYTLTDLMNEIKESSTKLKI 230
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlylpkldellddLSKELKVLKNVIRKPEPDLNQ 52
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
191-209 1.55e-03

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 39.19  E-value: 1.55e-03
                        10
                ....*....|....*....
gi 13543681 191 GITNLGNTCFFNAVMQNLA 209
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLS 19
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
190-213 6.79e-03

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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 37.64  E-value: 6.79e-03
                        10        20
                ....*....|....*....|....
gi 13543681 190 RGITNLGNTCFFNAVMQNLaqTYT 213
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCL--THT 23
 
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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