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Conserved domains on  [gi|7710078|ref|NP_057903|]
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E3 ubiquitin-protein ligase parkin [Mus musculus]

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List of domain hits

Name Accession Description Interval E-value
parkin_N cd01798
amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ...
3-72 2.90e-39

amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ubiquitin ligase with an amino-terminal ubiquitin-like (Ubl) domain and an RBR signature consisting of two RING finger domains separated by an IBR/DRIL domain. Naturally occurring mutations in parkin are thought to cause the disease AR_JP (autosomal-recessive juvenile parkinsonism). Parkin binds the Rpn10 subunit of 26S proteasomes through its Ubl domain.


:

Pssm-ID: 176393  Cd Length: 70  Bit Score: 137.18  E-value: 2.90e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078    3 VFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd01798   1 VYVRTNTGHTFPVEVDPDTDIKQLKEVVAKRQGVPPDQLRVIFAGKELRNTTTIQECDLGQQSILHAVRR 70
IBR smart00647
In Between Ring fingers; the domains occurs between pairs og RING fingers
313-374 5.34e-08

In Between Ring fingers; the domains occurs between pairs og RING fingers


:

Pssm-ID: 214763  Cd Length: 64  Bit Score: 49.72  E-value: 5.34e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710078     313 RYQQYGAEECVLQMGG-VLCPRPGCGAGLL--PEQGQRKVTCEGgnglgCGFVFCRDCKEAYHEG 374
Cdd:smart00647   2 KYERLLLESYVESNPDlKWCPAPDCSAAIIvtEEEGCNRVTCPK-----CGFSFCFRCKVPWHSP 61
IBR pfam01485
IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ...
411-452 1.95e-03

IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organisms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease.


:

Pssm-ID: 250654  Cd Length: 63  Bit Score: 36.42  E-value: 1.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 7710078    411 KKTTKPCPR--CNVPIEKNGGCMH-MKCPQpqCKLEWCWNCGCEW 452
Cdd:pfam01485  15 PKNLKWCPTpdCGNIIELTDGGSQnVTCSK--CGTEFCFLCKEPW 57
 
Name Accession Description Interval E-value
parkin_N cd01798
amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ...
3-72 2.90e-39

amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ubiquitin ligase with an amino-terminal ubiquitin-like (Ubl) domain and an RBR signature consisting of two RING finger domains separated by an IBR/DRIL domain. Naturally occurring mutations in parkin are thought to cause the disease AR_JP (autosomal-recessive juvenile parkinsonism). Parkin binds the Rpn10 subunit of 26S proteasomes through its Ubl domain.


Pssm-ID: 176393  Cd Length: 70  Bit Score: 137.18  E-value: 2.90e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078    3 VFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd01798   1 VYVRTNTGHTFPVEVDPDTDIKQLKEVVAKRQGVPPDQLRVIFAGKELRNTTTIQECDLGQQSILHAVRR 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 ...
13-74 1.75e-20

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 249708  Cd Length: 69  Bit Score: 85.37  E-value: 1.75e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710078     13 FPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRPR 74
Cdd:pfam00240   8 ITLEVDPSDTVLELKEKIEDKEGIPVDQQRLIYSGKVLEDDTTLSEYGIKDGSTLHLVLRLR 69
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
1-72 3.67e-15

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563  Cd Length: 72  Bit Score: 70.37  E-value: 3.67e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710078       1 MIVFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
IBR smart00647
In Between Ring fingers; the domains occurs between pairs og RING fingers
313-374 5.34e-08

In Between Ring fingers; the domains occurs between pairs og RING fingers


Pssm-ID: 214763  Cd Length: 64  Bit Score: 49.72  E-value: 5.34e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710078     313 RYQQYGAEECVLQMGG-VLCPRPGCGAGLL--PEQGQRKVTCEGgnglgCGFVFCRDCKEAYHEG 374
Cdd:smart00647   2 KYERLLLESYVESNPDlKWCPAPDCSAAIIvtEEEGCNRVTCPK-----CGFSFCFRCKVPWHSP 61
PTZ00044 PTZ00044
ubiquitin; Provisional
9-74 3.54e-06

ubiquitin; Provisional


Pssm-ID: 185411  Cd Length: 76  Bit Score: 44.82  E-value: 3.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7710078     9 SSYGFpvevDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRPR 74
Cdd:PTZ00044  13 QSFNF----EPDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSDYKVVPGSTIHMVLQLR 74
IBR pfam01485
IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ...
331-374 9.96e-05

IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organisms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease.


Pssm-ID: 250654  Cd Length: 63  Bit Score: 40.28  E-value: 9.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 7710078    331 CPRPGCGAGLLPEQG-QRKVTCEGgnglgCGFVFCRDCKEAYHEG 374
Cdd:pfam01485  21 CPTPDCGNIIELTDGgSQNVTCSK-----CGTEFCFLCKEPWHEG 60
IBR pfam01485
IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ...
411-452 1.95e-03

IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organisms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease.


Pssm-ID: 250654  Cd Length: 63  Bit Score: 36.42  E-value: 1.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 7710078    411 KKTTKPCPR--CNVPIEKNGGCMH-MKCPQpqCKLEWCWNCGCEW 452
Cdd:pfam01485  15 PKNLKWCPTpdCGNIIELTDGGSQnVTCSK--CGTEFCFLCKEPW 57
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
13-92 2.17e-05

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair].


Pssm-ID: 233045 [Multi-domain]  Cd Length: 378  Bit Score: 45.27  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078     13 FPVEVDSDTSILQLKEVVAKRQGV---PADQLRVIFAGKELPNHLTVQNCDL-EQQSIVHIVQRPRRrshETNASGGDEP 88
Cdd:TIGR00601  13 FKIDMEPDETVKELKEKIEAEQGKdayPVAQQKLIYSGKILSDDKTVKEYKIkEKDFVVVMVSKPKT---GTGKVAPPAA 89

                  ....
gi 7710078     89 QSTS 92
Cdd:TIGR00601  90 TPTS 93
 
Name Accession Description Interval E-value
parkin_N cd01798
amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ...
3-72 2.90e-39

amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ubiquitin ligase with an amino-terminal ubiquitin-like (Ubl) domain and an RBR signature consisting of two RING finger domains separated by an IBR/DRIL domain. Naturally occurring mutations in parkin are thought to cause the disease AR_JP (autosomal-recessive juvenile parkinsonism). Parkin binds the Rpn10 subunit of 26S proteasomes through its Ubl domain.


Pssm-ID: 176393  Cd Length: 70  Bit Score: 137.18  E-value: 2.90e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078    3 VFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd01798   1 VYVRTNTGHTFPVEVDPDTDIKQLKEVVAKRQGVPPDQLRVIFAGKELRNTTTIQECDLGQQSILHAVRR 70
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 ...
13-74 1.75e-20

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 249708  Cd Length: 69  Bit Score: 85.37  E-value: 1.75e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710078     13 FPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRPR 74
Cdd:pfam00240   8 ITLEVDPSDTVLELKEKIEDKEGIPVDQQRLIYSGKVLEDDTTLSEYGIKDGSTLHLVLRLR 69
UBL cd01769
Ubiquitin-like domain of UBL; UBLs function by remodeling the surface of their target proteins, ...
4-72 2.14e-16

Ubiquitin-like domain of UBL; UBLs function by remodeling the surface of their target proteins, changing their target's half-life, enzymatic activity, protein-protein interactions, subcellular localization or other properties. At least 10 different ubiquitin-like modifications exist in mammals, and attachment of different ubls to a target leads to different biological consequences. Ubl-conjugation cascades are initiated by activating enzymes, which also coordinate the ubls with their downstream pathways.


Pssm-ID: 176364  Cd Length: 69  Bit Score: 73.84  E-value: 2.14e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7710078    4 FVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd01769   1 TVKTLTGKTFELEVSPDDTVAELKAKIAAKEGVPPEQQRLIYAGKILKDDKTLSDYGIQDGSTLHLVLR 69
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
1-72 3.67e-15

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563  Cd Length: 72  Bit Score: 70.37  E-value: 3.67e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710078       1 MIVFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:smart00213   1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQDGSTIHLVLR 72
Ubiquitin cd01803
Ubiquitin; Ubiquitin (includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric ...
1-74 2.34e-10

Ubiquitin; Ubiquitin (includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric multiubiquitin protein chains)


Pssm-ID: 176398 [Multi-domain]  Cd Length: 76  Bit Score: 56.80  E-value: 2.34e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7710078    1 MIVFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRPR 74
Cdd:cd01803   1 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLR 74
UBQ cd00196
Ubiquitin-like proteins; Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. ...
4-72 3.85e-10

Ubiquitin-like proteins; Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. Ubiquitin-mediated proteolysis is part of the regulated turnover of proteins required for controlling cell cycle progression. Other family members are protein modifiers that perform a wide range of functions. Ubiquitination usually results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. The three-step mechanism requires an activating enzyme (E1) that forms a thiol ester with the C-terminal carboxy group, a conjugating enzyme (E2) that transiently carries the activated ubiquitin molecule as a thiol ester, and a ligase (E3) that transfers the activated ubiquitin from the E2 to the substrate lysine residue. In poly-ubiquitination, ubiquitin itself is the substrate.


Pssm-ID: 176352  Cd Length: 69  Bit Score: 55.99  E-value: 3.85e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7710078    4 FVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd00196   1 KVKLNDGKTVELLVPSGTTVADLKEKLAKKLGLPPEQQRLLVNGKILPDSLTLEDYGLQDGDELVLVPR 69
Nedd8 cd01806
Nebb8-like ubiquitin protein; Nedd8 (also known as Rub1) has a single conserved ...
1-70 4.85e-09

Nebb8-like ubiquitin protein; Nedd8 (also known as Rub1) has a single conserved ubiquitin-like domain that is part of a protein modification pathway similar to that of ubiquitin. Nedd8 modifies a family of molecular scaffold proteins called cullins that are responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis.


Pssm-ID: 176401  Cd Length: 76  Bit Score: 53.25  E-value: 4.85e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078    1 MIVFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIV 70
Cdd:cd01806   1 MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDDKTAADYKLEGGSVLHLV 70
Scythe_N cd01809
Ubiquitin-like domain of Scythe protein; Scythe protein (also known as Bat3) is an apoptotic ...
15-72 3.11e-08

Ubiquitin-like domain of Scythe protein; Scythe protein (also known as Bat3) is an apoptotic regulator that is highly conserved in eukaryotes and contains a ubiquitin-like domain near its N-terminus. Scythe binds reaper, a potent apoptotic inducer, and Scythe/Reaper are thought to signal apoptosis, in part through regulating the folding and activity of apoptotic signaling molecules.


Pssm-ID: 176404  Cd Length: 72  Bit Score: 50.69  E-value: 3.11e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7710078   15 VEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd01809  15 FTVEEEITVLDLKEKIAEEVGIPVEQQRLIYSGRVLKDDETLSEYKVEDGHTIHLVKR 72
IBR smart00647
In Between Ring fingers; the domains occurs between pairs og RING fingers
313-374 5.34e-08

In Between Ring fingers; the domains occurs between pairs og RING fingers


Pssm-ID: 214763  Cd Length: 64  Bit Score: 49.72  E-value: 5.34e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7710078     313 RYQQYGAEECVLQMGG-VLCPRPGCGAGLL--PEQGQRKVTCEGgnglgCGFVFCRDCKEAYHEG 374
Cdd:smart00647   2 KYERLLLESYVESNPDlKWCPAPDCSAAIIvtEEEGCNRVTCPK-----CGFSFCFRCKVPWHSP 61
RAD23_N cd01805
Ubiquitin-like domain of RAD23; RAD23 belongs to a family of adaptor molecules having affinity ...
1-74 9.85e-07

Ubiquitin-like domain of RAD23; RAD23 belongs to a family of adaptor molecules having affinity for both the proteasome and ubiquitinylated proteins and thought to shuttle these ubiquitinylated proteins to the proteasome for destruction. RAD23 interacts with ubiquitin through its C-terminal ubiquitin-associated domains (UBA) and with the proteasome through its N-terminal ubiquitin-like domain (UBL).


Pssm-ID: 176400  Cd Length: 77  Bit Score: 46.55  E-value: 9.85e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7710078    1 MIVFVRFNSSYGFPVEVDSDTSILQLKEVVAKRQG--VPADQLRVIFAGKELPNHLTVQNCDLEQQS-IVHIVQRPR 74
Cdd:cd01805   1 MKITFKTLKQQTFPIEVDPDDTVAELKEKIEEEKGcdYPPEQQKLIYSGKILKDDTTLEEYKIDEKDfVVVMVSKPK 77
Rad60-SLD pfam11976
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl ...
15-70 1.29e-06

Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl family member, and although SUMO-1 shares structural similarity to Ub, SUMO's cellular functions remain distinct insomuch as SUMO modification alters protein function through changes in activity, cellular localisation, or by protecting substrates from ubiquitination. Rad60 family members contain functionally enigmatic, integral SUMO-like domains (SLDs). Despite their divergence from SUMO, each Rad60 SLD interacts with a subset of SUMO pathway enzymes: SLD2 specifically binds the SUMO E2 conjugating enzyme (Ubc9)), whereas SLD1 binds the SUMO E1 (Fub2, also called Uba2) activating and E3 (Pli1, also called Siz1 and Siz2) specificity enzymes. Structural analysis of PDB:2uyz reveals a mechanistic basis for the near-synonymous roles of Rad60 and SUMO in survival of genotoxic stress and suggest unprecedented DNA-damage-response functions for SLDs in regulating SUMOylation. The Rad60 branch of this family is also known as RENi (Rad60-Esc2-Nip45), and biologically it should be two distinct families SUMO and RENi (Rad60-Esc2-Nip45).


Pssm-ID: 256771  Cd Length: 72  Bit Score: 45.97  E-value: 1.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 7710078     15 VEVDSDTSILQLKEVVAKRQGVPA-DQLRVIFAGKELPNHLTVQNCDLEQQSIVHIV 70
Cdd:pfam11976  15 IKVKPTTTLSKLINAYRKKKGIPEeQQVRLIFDGERLDPNDTVADYDIEDGDTIDVV 71
hPLIC_N cd01808
Ubiquitin-like domain of hPLIC-1 and hPLIC2; hPLIC-1 and hPLIC-2 (human homologs of the yeast ...
15-70 2.24e-06

Ubiquitin-like domain of hPLIC-1 and hPLIC2; hPLIC-1 and hPLIC-2 (human homologs of the yeast ubiquitin-like Dsk2 protein) are type2 UBL's (ubiquitin-like) proteins that are thought to serve as adaptors that link the ubiquitination machinery to the proteasome. The hPLIC's have an N-terminal UBL domain that binds the S5a subunit of the proteasome and a C-terminal UBA (ubiquitin-associated) domain that binds a ubiquitylated protein.


Pssm-ID: 176403  Cd Length: 71  Bit Score: 45.15  E-value: 2.24e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7710078   15 VEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIV 70
Cdd:cd01808  14 IEIAEDASVKDFKEAVSKKFKANQEQLVLIFAGKILKDTDTLTQHNIKDGLTVHLV 69
PTZ00044 PTZ00044
ubiquitin; Provisional
9-74 3.54e-06

ubiquitin; Provisional


Pssm-ID: 185411  Cd Length: 76  Bit Score: 44.82  E-value: 3.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7710078     9 SSYGFpvevDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRPR 74
Cdd:PTZ00044  13 QSFNF----EPDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSDYKVVPGSTIHMVLQLR 74
BAG1_N cd01812
Ubiquitin-like domain of BAG1; BAG1_N N-terminal ubiquitin-like (Ubl) domain of the BAG1 ...
14-71 5.43e-06

Ubiquitin-like domain of BAG1; BAG1_N N-terminal ubiquitin-like (Ubl) domain of the BAG1 protein. This domain occurs together with the BAG domain and is closely related to the Ubl domain of a family of deubiquitinases that includes Rpn11, UBP6 (USP14), USP7 (HAUSP).


Pssm-ID: 176407  Cd Length: 71  Bit Score: 44.22  E-value: 5.43e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7710078   14 PVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQ 71
Cdd:cd01812  13 DLSISSQATFGDLKKMLAPVTGVEPRDQKLIFKGKERDDAETLDMSGVKDGSKVMLLE 70
IBR pfam01485
IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ...
331-374 9.96e-05

IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organisms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease.


Pssm-ID: 250654  Cd Length: 63  Bit Score: 40.28  E-value: 9.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 7710078    331 CPRPGCGAGLLPEQG-QRKVTCEGgnglgCGFVFCRDCKEAYHEG 374
Cdd:pfam01485  21 CPTPDCGNIIELTDGgSQNVTCSK-----CGTEFCFLCKEPWHEG 60
Fubi cd01793
Fubi ubiquitin-like protein; Fubi is a ubiquitin-like protein encoded by the fau gene which ...
1-72 1.18e-03

Fubi ubiquitin-like protein; Fubi is a ubiquitin-like protein encoded by the fau gene which has an N-terminal ubiquitin-like domain (also referred to as FUBI) fused to the ribosomal protein S30. Fubi is thought to be a tumor suppressor protein and the FUBI domain may act as a substitute or an inhibitor of ubiquitin or one of ubiquitin's close relatives UCRP, FAT10, and Nedd8.


Pssm-ID: 176388  Cd Length: 74  Bit Score: 37.05  E-value: 1.18e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710078    1 MIVFVRFNSSYGFpvEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQR 72
Cdd:cd01793   1 MQLFVRAQNTHTL--EVTGQETVSDIKAHVAGLEGIDVEDQVLLLAGVPLEDDATLGQCGVEELCTLEVAGR 70
IBR pfam01485
IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ...
411-452 1.95e-03

IBR domain; The IBR (In Between Ring fingers) domain is often found to occur between pairs of ring fingers (pfam00097). This domain has also been called the C6HC domain and DRIL (for double RING finger linked) domain. Proteins that contain two Ring fingers and an IBR domain (these proteins are also termed RBR family proteins) are thought to exist in all eukaryotic organisms. RBR family members play roles in protein quality control and can indirectly regulate transcription. Evidence suggests that RBR proteins are often parts of cullin-containing ubiquitin ligase complexes. The ubiquitin ligase Parkin is an RBR family protein whose mutations are involved in forms of familial Parkinson's disease.


Pssm-ID: 250654  Cd Length: 63  Bit Score: 36.42  E-value: 1.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 7710078    411 KKTTKPCPR--CNVPIEKNGGCMH-MKCPQpqCKLEWCWNCGCEW 452
Cdd:pfam01485  15 PKNLKWCPTpdCGNIIELTDGGSQnVTCSK--CGTEFCFLCKEPW 57
GDX_N cd01807
ubiquitin-like domain of GDX; GDX contains an N-terminal ubiquitin-like domain as well as an ...
15-73 2.05e-03

ubiquitin-like domain of GDX; GDX contains an N-terminal ubiquitin-like domain as well as an uncharacterized c-terminal domain. The function of GDX is unknown.


Pssm-ID: 176402  Cd Length: 74  Bit Score: 36.42  E-value: 2.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7710078   15 VEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKELPNHLTVQNCDLEQQSIVHIVQRP 73
Cdd:cd01807  15 LQVSEKESVSTLKKLVSEHLNVPEEQQRLLFKGKALADDKRLSDYSIGPNAKLNLVVRP 73
DDI1_N cd01796
DNA damage inducible protein 1 ubiquitin-like domain; DDI1_N DDI1 (DNA damage inducible ...
13-71 4.67e-03

DNA damage inducible protein 1 ubiquitin-like domain; DDI1_N DDI1 (DNA damage inducible protein 1) has an amino-terminal ubiquitin-like domain, an retroviral protease-like (RVP-like) domain, and a UBA (ubiquitin-associated) domain. This CD represents the amino-terminal ubiquitin-like domain of DDI1.


Pssm-ID: 176391  Cd Length: 71  Bit Score: 35.42  E-value: 4.67e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078   13 FPVEVDSDTSILQLKEVVAKRQGVPADQLRVIFAGKEL-PNHLTVQNCDLEQQSIVHIVQ 71
Cdd:cd01796  12 FSLDVDPDLELENFKALCEAESGIPASQQQLIYNGRELvDNKRLLALYGVKDGDLVVLRQ 71
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
13-92 2.17e-05

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University) [DNA metabolism, DNA replication, recombination, and repair].


Pssm-ID: 233045 [Multi-domain]  Cd Length: 378  Bit Score: 45.27  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710078     13 FPVEVDSDTSILQLKEVVAKRQGV---PADQLRVIFAGKELPNHLTVQNCDL-EQQSIVHIVQRPRRrshETNASGGDEP 88
Cdd:TIGR00601  13 FKIDMEPDETVKELKEKIEAEQGKdayPVAQQKLIYSGKILSDDKTVKEYKIkEKDFVVVMVSKPKT---GTGKVAPPAA 89

                  ....
gi 7710078     89 QSTS 92
Cdd:TIGR00601  90 TPTS 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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