NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|33147082|ref|NP_476512|]
View 

large proline-rich protein BAG6 isoform 1 [Mus musculus]

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DUF3538 pfam12057
Domain of unknown function (DUF3538); This presumed domain is functionally uncharacterized. ...
278-392 2.71e-47

Domain of unknown function (DUF3538); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 120 amino acids in length. This domain is found associated with pfam00240. This domain has a conserved SDL sequence motif.


:

Pssm-ID: 288877  Cd Length: 115  Bit Score: 166.02  E-value: 2.71e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    278 VEVLQELQRLQRRLQPFLQRYCEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLH 357
Cdd:pfam12057    2 AEVLQELRRVQERLRPFLERYHSILNEDPTFDYNNGTEGREEDQRILDRVSEALHLLSHAYHALSDLRLNLSQPPPRHLH 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 33147082    358 vVRPMSHYTTPmVLQQAAIPIQINVGTTVTMTGNG 392
Cdd:pfam12057   82 -CRPMLHQQSA-VLLSGIAPIQVNLGVTLTMASNG 114
Scythe_N cd01809
Ubiquitin-like domain of Scythe protein; Scythe protein (also known as Bat3) is an apoptotic ...
17-87 2.22e-31

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: 119.25  E-value: 2.22e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082   17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLVER 87
Cdd:cd01809    1 IEIKVKTLDSQTHTFTVEEEITVLDLKEKIAEEVGIPVEQQRLIYSGRVLKDDETLSEYKVeDGHTIHLVKR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
17-87 1.09e-20

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


:

Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 88.47  E-value: 1.09e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082      17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVER 87
Cdd:smart00213    1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQdGSTIHLVLR 72
 
Name Accession Description Interval E-value
DUF3538 pfam12057
Domain of unknown function (DUF3538); This presumed domain is functionally uncharacterized. ...
278-392 2.71e-47

Domain of unknown function (DUF3538); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 120 amino acids in length. This domain is found associated with pfam00240. This domain has a conserved SDL sequence motif.


Pssm-ID: 288877  Cd Length: 115  Bit Score: 166.02  E-value: 2.71e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    278 VEVLQELQRLQRRLQPFLQRYCEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLH 357
Cdd:pfam12057    2 AEVLQELRRVQERLRPFLERYHSILNEDPTFDYNNGTEGREEDQRILDRVSEALHLLSHAYHALSDLRLNLSQPPPRHLH 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 33147082    358 vVRPMSHYTTPmVLQQAAIPIQINVGTTVTMTGNG 392
Cdd:pfam12057   82 -CRPMLHQQSA-VLLSGIAPIQVNLGVTLTMASNG 114
Scythe_N cd01809
Ubiquitin-like domain of Scythe protein; Scythe protein (also known as Bat3) is an apoptotic ...
17-87 2.22e-31

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: 119.25  E-value: 2.22e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082   17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLVER 87
Cdd:cd01809    1 IEIKVKTLDSQTHTFTVEEEITVLDLKEKIAEEVGIPVEQQRLIYSGRVLKDDETLSEYKVeDGHTIHLVKR 72
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 ...
22-89 5.77e-14

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: 278661  Cd Length: 69  Bit Score: 68.81  E-value: 5.77e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33147082     22 KTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVERAP 89
Cdd:pfam00240    1 KTLDGKTITLEVKPSDTVLELKEKIEEREGVPPSQQRLIYKGKVLEDDTTLSEYGIEdGSTLHLVLRLR 69
PTZ00044 PTZ00044
ubiquitin; Provisional
17-85 2.39e-07

ubiquitin; Provisional


Pssm-ID: 185411  Cd Length: 76  Bit Score: 49.82  E-value: 2.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLV 85
Cdd:PTZ00044    1 MQILIKTLTGKKQSFNFEPDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSDYKVvPGSTIHMV 70
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
17-87 1.09e-20

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


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 88.47  E-value: 1.09e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082      17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVER 87
Cdd:smart00213    1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQdGSTIHLVLR 72
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
17-124 1.18e-07

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: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 54.13  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082     17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVS---IPSEKQRLIYQGRVLQDDKKLQEYNV--GGKVIHLVER---- 87
Cdd:TIGR00601    1 MTLTFKTLQQQKFKIDMEPDETVKELKEKIEAEQGkdaYPVAQQKLIYSGKILSDDKTVKEYKIkeKDFVVVMVSKpktg 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 33147082     88 ----APPQTQLPSGASSGTGSASATHGG--APLPGTRGPGASV 124
Cdd:TIGR00601   81 tgkvAPPAATPTSAPTPTPSPPASPASGmsAAPASAVEEKSPS 123
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
927-1118 1.65e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   927 GVNPSLVSWLTTMMGLRLQVVLEhmpVGPDAILRYVRRVGDPPQTLPEEPMEVQGAERTSPEPQRENASPAPGTTAEEAM 1006
Cdd:PRK07764  565 GNAEVLVTALAEELGGDWQVEAV---VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASA 641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082  1007 SRGPPPAPEGGSRDEQDGASADAEPWAAAVP-----PEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGP 1081
Cdd:PRK07764  642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKaggaaPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP 721
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 33147082  1082 QLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQE 1118
Cdd:PRK07764  722 PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758
CF222 pfam15661
C6orf222, uncharacterized family; This family of proteins is found in eukaryotes. Proteins in ...
973-1118 3.08e-04

C6orf222, uncharacterized family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 618 and 652 amino acids in length.


Pssm-ID: 292289 [Multi-domain]  Cd Length: 648  Bit Score: 43.34  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    973 PEEPMEVQGAERTSPEPQRENASPAPGTtaEEAmsrGPPPAPEGGSRD--------EQDGASA-DAEPWAAAVPPEWVP- 1042
Cdd:pfam15661  161 AEETKGAQDQEAEGQEAGLPKLAAASRS--EEA---DLGPAPRGGEDSdlhqslliEGGGAGAsDVSPQATGHQQEEELr 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   1043 ------IIQQDIQSQRKVKPQ--------PPLSDAYLSGMPAKRRKTMQGEGP---QLLLSEAVSRAAKAAGARPLTSPE 1105
Cdd:pfam15661  236 kpdqdaIIQMIVELLQKVGDQweeeqlqaPQPEVAPQNPAPVVRKKSQEKKSSlkrAFSHKKHSSEEPKRAGAADVSSPE 315
                          170       180       190
                   ....*....|....*....|....*....|....
gi 33147082   1106 ---------------------SLSRDLEAPEVQE 1118
Cdd:pfam15661  316 srppkrpsflplcvgghrpsiSSSPGLEEPEVQE 349
 
Name Accession Description Interval E-value
DUF3538 pfam12057
Domain of unknown function (DUF3538); This presumed domain is functionally uncharacterized. ...
278-392 2.71e-47

Domain of unknown function (DUF3538); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 120 amino acids in length. This domain is found associated with pfam00240. This domain has a conserved SDL sequence motif.


Pssm-ID: 288877  Cd Length: 115  Bit Score: 166.02  E-value: 2.71e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    278 VEVLQELQRLQRRLQPFLQRYCEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLH 357
Cdd:pfam12057    2 AEVLQELRRVQERLRPFLERYHSILNEDPTFDYNNGTEGREEDQRILDRVSEALHLLSHAYHALSDLRLNLSQPPPRHLH 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 33147082    358 vVRPMSHYTTPmVLQQAAIPIQINVGTTVTMTGNG 392
Cdd:pfam12057   82 -CRPMLHQQSA-VLLSGIAPIQVNLGVTLTMASNG 114
Scythe_N cd01809
Ubiquitin-like domain of Scythe protein; Scythe protein (also known as Bat3) is an apoptotic ...
17-87 2.22e-31

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: 119.25  E-value: 2.22e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082   17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLVER 87
Cdd:cd01809    1 IEIKVKTLDSQTHTFTVEEEITVLDLKEKIAEEVGIPVEQQRLIYSGRVLKDDETLSEYKVeDGHTIHLVKR 72
UBL cd01769
Ubiquitin-like domain of UBL; UBLs function by remodeling the surface of their target proteins, ...
20-87 3.13e-19

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: 84.24  E-value: 3.13e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33147082   20 LVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVER 87
Cdd:cd01769    1 TVKTLTGKTFELEVSPDDTVAELKAKIAAKEGVPPEQQRLIYAGKILKDDKTLSDYGIQdGSTLHLVLR 69
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 ...
22-89 5.77e-14

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: 278661  Cd Length: 69  Bit Score: 68.81  E-value: 5.77e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33147082     22 KTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVERAP 89
Cdd:pfam00240    1 KTLDGKTITLEVKPSDTVLELKEKIEEREGVPPSQQRLIYKGKVLEDDTTLSEYGIEdGSTLHLVLRLR 69
UBQ cd00196
Ubiquitin-like proteins; Ubiquitin homologs; Includes ubiquitin and ubiquitin-like proteins. ...
21-87 2.61e-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: 58.31  E-value: 2.61e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33147082   21 VKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLVER 87
Cdd:cd00196    2 VKLNDGKTVELLVPSGTTVADLKEKLAKKLGLPPEQQRLLVNGKILPDSLTLEDYGLqDGDELVLVPR 69
RAD23_N cd01805
Ubiquitin-like domain of RAD23; RAD23 belongs to a family of adaptor molecules having affinity ...
19-77 6.08e-10

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: 57.34  E-value: 6.08e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33147082   19 VLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVS--IPSEKQRLIYQGRVLQDDKKLQEYNV 77
Cdd:cd01805    3 ITFKTLKQQTFPIEVDPDDTVAELKEKIEEEKGcdYPPEQQKLIYSGKILKDDTTLEEYKI 63
Ubiquitin cd01803
Ubiquitin; Ubiquitin (includes Ubq/RPL40e and Ubq/RPS27a fusions as well as homopolymeric ...
17-87 5.95e-08

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: 51.79  E-value: 5.95e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082   17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGK-VIHLVER 87
Cdd:cd01803    1 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKEsTLHLVLR 72
Nedd8 cd01806
Nebb8-like ubiquitin protein; Nedd8 (also known as Rub1) has a single conserved ...
19-85 2.26e-07

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 [Multi-domain]  Cd Length: 76  Bit Score: 49.78  E-value: 2.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33147082   19 VLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLV 85
Cdd:cd01806    3 IKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDDKTAADYKLeGGSVLHLV 70
PTZ00044 PTZ00044
ubiquitin; Provisional
17-85 2.39e-07

ubiquitin; Provisional


Pssm-ID: 185411  Cd Length: 76  Bit Score: 49.82  E-value: 2.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLV 85
Cdd:PTZ00044    1 MQILIKTLTGKKQSFNFEPDNTVQQVKMALQEKEGIDVKQIRLIYSGKQMSDDLKLSDYKVvPGSTIHMV 70
SF3a120_C cd01800
Ubiquitin-like domain of Mammalian splicing factor SF3a_120; SF3a120_C Mammalian splicing ...
24-84 2.31e-05

Ubiquitin-like domain of Mammalian splicing factor SF3a_120; SF3a120_C Mammalian splicing factor SF3a consists of three subunits of 60, 66, and 120 kDa and functions early during pre-mRNA splicing by converting the U2 snRNP to its active form. The 120kDa subunit (SF3a120) has a carboxy-terminal ubiquitin-like domain and two SWAP (suppressor-of-white-apricot) domains, referred to collectively as the SURP module, at its amino-terminus.


Pssm-ID: 176395  Cd Length: 76  Bit Score: 43.98  E-value: 2.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082   24 LDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHL 84
Cdd:cd01800    5 LNGQMLNFTLQLSDPVSVLKVKIHEETGMPAGKQKLQYEGIFIKDSNSLAYYNLAnGTIIHL 66
GDX_N cd01807
ubiquitin-like domain of GDX; GDX contains an N-terminal ubiquitin-like domain as well as an ...
21-89 3.53e-05

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: 43.35  E-value: 3.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   21 VKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKV-IHLVERAP 89
Cdd:cd01807    5 VKLLQGRECSLQVSEKESVSTLKKLVSEHLNVPEEQQRLLFKGKALADDKRLSDYSIGPNAkLNLVVRPP 74
hPLIC_N cd01808
Ubiquitin-like domain of hPLIC-1 and hPLIC2; hPLIC-1 and hPLIC-2 (human homologs of the yeast ...
17-85 5.21e-05

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: 42.84  E-value: 5.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   17 LEVLVKTlDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLV 85
Cdd:cd01808    1 IKVTVKT-PKDKEEIEIAEDASVKDFKEAVSKKFKANQEQLVLIFAGKILKDTDTLTQHNIKdGLTVHLV 69
parkin_N cd01798
amino-terminal ubiquitin-like of parkin protein; parkin_N parkin protein is a RING-type E3 ...
19-87 6.79e-05

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: 42.42  E-value: 6.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   19 VLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVER 87
Cdd:cd01798    1 VYVRTNTGHTFPVEVDPDTDIKQLKEVVAKRQGVPPDQLRVIFAGKELRNTTTIQECDLGqQSILHAVRR 70
NIRF_N cd01797
amino-terminal ubiquitin-like domain of Np95 and NIRF; NIRF_N This CD represents the ...
21-90 2.15e-04

amino-terminal ubiquitin-like domain of Np95 and NIRF; NIRF_N This CD represents the amino-terminal ubiquitin-like domain of a family of nuclear proteins that includes Np95 and NIRF (Np95/ICBP90-like RING finger) protein. Both Np95 and NIRF have a domain architecture consisting of a ubiquitin-like domain, a PHD finger, a YDG/SRA domain, Rb-binding motifs and a RING finger domain. Both Np95 and NIRF are ubiquitin ligases that ubiquitinate PCNP (PEST-containing nuclear proteins). While Np95 is capable of binding histones, NIRF is involved in cell cycle regulation.


Pssm-ID: 176392  Cd Length: 78  Bit Score: 40.96  E-value: 2.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33147082   21 VKTLD-SQTRTF-IVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVERAPP 90
Cdd:cd01797    5 VRTMDgKETRTVdSLSRLTKVEELREKIQELFNVEPECQRLFYRGKQMEDGHTLFDYNVGlNDIIQLLVRQDP 77
Rad60-SLD pfam11976
Ubiquitin-2 like Rad60 SUMO-like; The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl ...
17-85 4.00e-03

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 localization, 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: 288803  Cd Length: 72  Bit Score: 36.75  E-value: 4.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33147082     17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIP-SEKQRLIYQGRVLQDDKKLQEYNV-GGKVIHLV 85
Cdd:pfam11976    1 INIKLKGKDGKEVFIKVKPTTTVSKLINAYRKKRGIPeSQQVRLLFDGERLDPNSTVADLDIeDGDTIDVV 71
Rad60-SLD_2 pfam13881
Ubiquitin-2 like Rad60 SUMO-like;
37-90 5.90e-03

Ubiquitin-2 like Rad60 SUMO-like;


Pssm-ID: 290592  Cd Length: 111  Bit Score: 36.52  E-value: 5.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082     37 MNVKEFKEHIAASvsIPSEKQ---------RLIYQGRVLQDDKKLQEY-----NVGGKVI--HLVERAPP 90
Cdd:pfam13881   24 TTVADLKEKVIAQ--WPKDKEegpktvndvKLINAGKILENNKTLGECrlpfgETPGGVTtmHVVVRPPL 91
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
17-87 1.09e-20

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


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 88.47  E-value: 1.09e-20
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33147082      17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVG-GKVIHLVER 87
Cdd:smart00213    1 IELTVKTLDGKTITLEVKPSDTVSELKEKIAELTGIPPEQQRLIYKGKVLEDDRTLADYGIQdGSTIHLVLR 72
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
17-124 1.18e-07

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: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 54.13  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082     17 LEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVS---IPSEKQRLIYQGRVLQDDKKLQEYNV--GGKVIHLVER---- 87
Cdd:TIGR00601    1 MTLTFKTLQQQKFKIDMEPDETVKELKEKIEAEQGkdaYPVAQQKLIYSGKILSDDKTVKEYKIkeKDFVVVMVSKpktg 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 33147082     88 ----APPQTQLPSGASSGTGSASATHGG--APLPGTRGPGASV 124
Cdd:TIGR00601   81 tgkvAPPAATPTSAPTPTPSPPASPASGmsAAPASAVEEKSPS 123
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
927-1118 1.65e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   927 GVNPSLVSWLTTMMGLRLQVVLEhmpVGPDAILRYVRRVGDPPQTLPEEPMEVQGAERTSPEPQRENASPAPGTTAEEAM 1006
Cdd:PRK07764  565 GNAEVLVTALAEELGGDWQVEAV---VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASA 641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082  1007 SRGPPPAPEGGSRDEQDGASADAEPWAAAVP-----PEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGP 1081
Cdd:PRK07764  642 APAPGVAAPEHHPKHVAVPDASDGGDGWPAKaggaaPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP 721
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 33147082  1082 QLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQE 1118
Cdd:PRK07764  722 PQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758
CF222 pfam15661
C6orf222, uncharacterized family; This family of proteins is found in eukaryotes. Proteins in ...
973-1118 3.08e-04

C6orf222, uncharacterized family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 618 and 652 amino acids in length.


Pssm-ID: 292289 [Multi-domain]  Cd Length: 648  Bit Score: 43.34  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082    973 PEEPMEVQGAERTSPEPQRENASPAPGTtaEEAmsrGPPPAPEGGSRD--------EQDGASA-DAEPWAAAVPPEWVP- 1042
Cdd:pfam15661  161 AEETKGAQDQEAEGQEAGLPKLAAASRS--EEA---DLGPAPRGGEDSdlhqslliEGGGAGAsDVSPQATGHQQEEELr 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   1043 ------IIQQDIQSQRKVKPQ--------PPLSDAYLSGMPAKRRKTMQGEGP---QLLLSEAVSRAAKAAGARPLTSPE 1105
Cdd:pfam15661  236 kpdqdaIIQMIVELLQKVGDQweeeqlqaPQPEVAPQNPAPVVRKKSQEKKSSlkrAFSHKKHSSEEPKRAGAADVSSPE 315
                          170       180       190
                   ....*....|....*....|....*....|....
gi 33147082   1106 ---------------------SLSRDLEAPEVQE 1118
Cdd:pfam15661  316 srppkrpsflplcvgghrpsiSSSPGLEEPEVQE 349
PHA03247 PHA03247
large tegument protein UL36; Provisional
962-1154 1.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082   962 VRRVGDPPqtlPEEPMEVQGAERTSPEPQRENASPAPGTTAEEAMSRG-------------PPPAPEGGSRDEQDGASAD 1028
Cdd:PHA03247 2883 VRRLARPA---VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPqpqppppppprpqPPLAPTTDPAGAGEPSGAV 2959
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33147082  1029 AEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRrktmqgegpqlLLSEAVSRAAKAAGARPltsPESLS 1108
Cdd:PHA03247 2960 PQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR-----------VSSWASSLALHEETDPP---PVSLK 3025
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 33147082  1109 RDLEAP-EVQESYRQQLRSDIQKRLQE---DPNYSPQRFPNAHRAFADDP 1154
Cdd:PHA03247 3026 QTLWPPdDTEDSDADSLFDSDSERSDLealDPLPPEPHDPFAHEPDPATP 3075
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH