NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|389886556|ref|NP_001254513|]
View 

RING finger protein 37 isoform c [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DUF5918 pfam19318
Family of unknown function (DUF5918); This family represents the N-terminal domain of the RING ...
4-217 2.20e-109

Family of unknown function (DUF5918); This family represents the N-terminal domain of the RING finger protein 37 (RNF37), an U-box domain-containing protein. This is a variable region that probably has a role in function regulation.


:

Pssm-ID: 466039  Cd Length: 211  Bit Score: 323.83  E-value: 2.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556    4 NLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAgGGQNVTGLEM 83
Cdd:pfam19318   1 NLCLPQFGTRIHCNKVCADGYEVTNLISEDLSKRRRGFRAEYFIKPPVDITLSFPFPIEICRIDVDPKV-GGQASKGLEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556   84 YTSASSSRvSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGamEATLPSPAVVAQ-ELWNK 162
Cdd:pfam19318  80 FTSSDSSS-SWNSQSRLSSSSSTQSFEDEPIFTLVGRCELKEETKVCFSNRRFRPRPPFH--SAPPPSPANCRQeELWSR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 389886556  163 GALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENL 217
Cdd:pfam19318 157 GLQSLSAVTHLRVRIPKTGGGSVPGIKRLEIWGQPARSCPAELVEKILDVHSKSE 211
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
260-312 6.16e-30

U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.


:

Pssm-ID: 438322  Cd Length: 53  Bit Score: 110.87  E-value: 6.16e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389886556 260 PEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAF 312
Cdd:cd16660    1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEATWGRLPSDPFTGVPF 53
 
Name Accession Description Interval E-value
DUF5918 pfam19318
Family of unknown function (DUF5918); This family represents the N-terminal domain of the RING ...
4-217 2.20e-109

Family of unknown function (DUF5918); This family represents the N-terminal domain of the RING finger protein 37 (RNF37), an U-box domain-containing protein. This is a variable region that probably has a role in function regulation.


Pssm-ID: 466039  Cd Length: 211  Bit Score: 323.83  E-value: 2.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556    4 NLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAgGGQNVTGLEM 83
Cdd:pfam19318   1 NLCLPQFGTRIHCNKVCADGYEVTNLISEDLSKRRRGFRAEYFIKPPVDITLSFPFPIEICRIDVDPKV-GGQASKGLEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556   84 YTSASSSRvSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGamEATLPSPAVVAQ-ELWNK 162
Cdd:pfam19318  80 FTSSDSSS-SWNSQSRLSSSSSTQSFEDEPIFTLVGRCELKEETKVCFSNRRFRPRPPFH--SAPPPSPANCRQeELWSR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 389886556  163 GALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENL 217
Cdd:pfam19318 157 GLQSLSAVTHLRVRIPKTGGGSVPGIKRLEIWGQPARSCPAELVEKILDVHSKSE 211
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
260-312 6.16e-30

U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.


Pssm-ID: 438322  Cd Length: 53  Bit Score: 110.87  E-value: 6.16e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389886556 260 PEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAF 312
Cdd:cd16660    1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEATWGRLPSDPFTGVPF 53
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
259-337 3.78e-28

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 106.63  E-value: 3.78e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389886556  259 VPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEatwgrVPSDPFTgVAFTPHSQPLPHPSLKARIDHFLLQHSI 337
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSV-----DPTDPFT-REPLTHDQLIPNLELKAKIDAWLEEKRW 73
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
262-331 9.58e-15

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 68.80  E-value: 9.58e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556   262 EFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSeatwgrVPSDPFTGVAFTpHSQPLPHPSLKARIDHF 331
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLS------HGTDPVTGQPLT-HEDLIPNLALKSAIQEW 63
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
254-334 1.45e-05

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 47.67  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556 254 EIIQDVPEEFLDPITLEIMPCPMLLPSGKV-IDQSTLEKCNRSEATwgrvpsDPFTGVAFTpHSQPLPHPSLKARIDHFL 332
Cdd:COG5113  846 EDMGDVPDEFLDPLMFTIMKDPVKLPTSRItIDRSTIKAHLLSDGT------DPFNRMPLT-LDDVTPNAELREKINRFY 918

                 ..
gi 389886556 333 LQ 334
Cdd:COG5113  919 KC 920
 
Name Accession Description Interval E-value
DUF5918 pfam19318
Family of unknown function (DUF5918); This family represents the N-terminal domain of the RING ...
4-217 2.20e-109

Family of unknown function (DUF5918); This family represents the N-terminal domain of the RING finger protein 37 (RNF37), an U-box domain-containing protein. This is a variable region that probably has a role in function regulation.


Pssm-ID: 466039  Cd Length: 211  Bit Score: 323.83  E-value: 2.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556    4 NLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAgGGQNVTGLEM 83
Cdd:pfam19318   1 NLCLPQFGTRIHCNKVCADGYEVTNLISEDLSKRRRGFRAEYFIKPPVDITLSFPFPIEICRIDVDPKV-GGQASKGLEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556   84 YTSASSSRvSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGamEATLPSPAVVAQ-ELWNK 162
Cdd:pfam19318  80 FTSSDSSS-SWNSQSRLSSSSSTQSFEDEPIFTLVGRCELKEETKVCFSNRRFRPRPPFH--SAPPPSPANCRQeELWSR 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 389886556  163 GALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENL 217
Cdd:pfam19318 157 GLQSLSAVTHLRVRIPKTGGGSVPGIKRLEIWGQPARSCPAELVEKILDVHSKSE 211
RING-Ubox_RNF37 cd16660
U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also ...
260-312 6.16e-30

U-box domain, a modified RING finger, found in RING finger protein 37 (RNF37); RNF37, also known as KIAA0860, U-box domain-containing protein 5 (UBOX5), UbcM4-interacting protein 5 (UIP5), or ubiquitin-conjugating enzyme 7-interacting protein 5, is an E3 ubiquitin-protein ligase found exclusively in the nucleus as part of a nuclear dot-like structure. It interacts with the molecular chaperone VCP/p97 protein. RNF37 contains a U-box domain followed by a potential nuclear location signal (NLS), and a C-terminal C3HC4-type RING-HC finger. The U-box domain is a modified RING finger domain that lacks the hallmark metal-chelating cysteines and histidines of the latter, but is likely to adopt a RING finger-like conformation. The presence of the U-box, but not of the RING finger, is required for the E3 activity. The U-box domain can directly interact with several E2 enzymes, including UbcM2, UbcM3, UbcM4, UbcH5, and UbcH8, suggesting a similar function as the RING finger in the ubiquitination pathway. This model corresponds to the U-box domain.


Pssm-ID: 438322  Cd Length: 53  Bit Score: 110.87  E-value: 6.16e-30
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389886556 260 PEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAF 312
Cdd:cd16660    1 PEEFLDPITCELMTLPVLLPSGKVVDQSTLEKYIKEEATWGRLPSDPFTGVPF 53
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
259-337 3.78e-28

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 106.63  E-value: 3.78e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389886556  259 VPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEatwgrVPSDPFTgVAFTPHSQPLPHPSLKARIDHFLLQHSI 337
Cdd:pfam04564   1 IPDEFLDPITFELMTDPVILPSGITYDRSTIERHLLSV-----DPTDPFT-REPLTHDQLIPNLELKAKIDAWLEEKRW 73
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
262-331 9.58e-15

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 68.80  E-value: 9.58e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556   262 EFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSeatwgrVPSDPFTGVAFTpHSQPLPHPSLKARIDHF 331
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLS------HGTDPVTGQPLT-HEDLIPNLALKSAIQEW 63
RING-Ubox_UBE4B cd16658
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and ...
258-332 2.15e-12

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 B (UBE4B) and similar proteins; UBE4B, also known as UFD2a, is a U-box-type ubiquitin-protein ligase that functions as an E3 ubiquitin ligase and an E4 polyubiquitin chain elongation factor, which catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain. It is a mammalian homolog of yeast UFD2 ubiquitination factor and it participates in the proteasomal degradation of misfolded or damaged proteins through association with chaperones. It is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. UBE4B has contradictory functions upon tumorigenesis as an oncogene or tumor suppressor in different types of cancers. It is essential for Hdm2 (also known as Mdm2)-mediated p53 degradation. It mediates p53 polyubiquitination and degradation, as well as inhibits p53-dependent transactivation and apoptosis, and thus plays an important role in regulating phosphorylated p53 following DNA damage. UBE4B is also associated with other pathways independent of the p53 family, such as polyglutamine aggregation and Wallerian degeneration, both of which are critical in neurodegenerative diseases. Moreover, UBE4B acts as a regulator of epidermal growth factor receptor (EGFR) degradation. It is recruited to endosomes in response to EGFR activation by binding to Hrs, a key component of endosomal sorting complex required for transport (ESCRT) 0, and then regulates endosomal sorting, affecting cellular levels of the EGFR and its downstream signaling. UBE4B contains a ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438320  Cd Length: 74  Bit Score: 62.29  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556 258 DVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEatwgrvPSDPFTgvaftphSQPL------PHPSLKARIDHF 331
Cdd:cd16658    3 DAPDEFLDPLMDTLMTDPVILPSGTIMDRSIILRHLLNS------QTDPFN-------RQPLtedmlePVPELKERIQAW 69

                 .
gi 389886556 332 L 332
Cdd:cd16658   70 I 70
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
263-312 5.30e-11

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 57.56  E-value: 5.30e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 389886556 263 FLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEatwgrvPSDPFTGVAF 312
Cdd:cd16453    1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSD------NTDPFTREPL 44
RING-Ubox_UBE4A cd16657
U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and ...
261-335 2.07e-10

U-box domain, a modified RING finger, found in ubiquitin conjugation factor E4 A (UBE4A) and similar proteins; This subfamily includes yeast ubiquitin fusion degradation protein 2 (UFD2p) and its mammalian homolog, UBE4A. Yeast UFD2p, also known as ubiquitin conjugation factor E4 or UB fusion protein 2, is a polyubiquitin chain conjugation factor (E4) in the ubiquitin fusion degradation (UFD) pathway which catalyzes elongation of the ubiquitin chain through Lys48 linkage. It binds to substrates conjugated with one to three ubiquitin molecules and catalyzes the addition of further ubiquitin moieties in the presence of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2) and ubiquitin ligase (E3), yielding multiubiquitylated substrates that are targets for the 26S proteasome. UFD2p is implicated in cell survival under stress conditions and is essential for homoeostasis of unsaturated fatty acids. It interacts with UBL-UBA proteins Rad23 and Dsk2, which are involved in the endoplasmic reticulum-associated degradation, ubiquitin fusion degradation, and OLE-1 gene induction pathways. UBE4A is a U-box-type ubiquitin-protein ligase that is located in common neuroblastoma deletion regions and may be subject to mutations in tumors. It may have a specific role in different biochemical processes other than ubiquitination, including growth or differentiation. Members of this family contain an N-terminal ubiquitin elongating factor core and a RING-like U-box domain at the C-terminus.


Pssm-ID: 438319  Cd Length: 70  Bit Score: 56.51  E-value: 2.07e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 389886556 261 EEFLDPITLEIMPCPMLLPSGKV-IDQSTLEKCNRSEATwgrvpsDPFTGVAFTPhSQPLPHPSLKARIDHFLLQH 335
Cdd:cd16657    1 DEFLDPIMYTLMKDPVILPSSKVtVDRSTIKRHLLSDQT------DPFNRSPLTL-DMVIPNEELKQKIEEFLAEK 69
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
259-335 8.95e-06

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 43.33  E-value: 8.95e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389886556 259 VPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWgrvpsDPFTGVAFTPhSQPLPHPSLKARIDHFLLQH 335
Cdd:cd16654    1 VPDYLCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHF-----DPITREPLTQ-DQLIPNLALKEAIEAFLEEN 71
UFD2 COG5113
Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, ...
254-334 1.45e-05

Ubiquitin fusion degradation protein 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227444 [Multi-domain]  Cd Length: 929  Bit Score: 47.67  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886556 254 EIIQDVPEEFLDPITLEIMPCPMLLPSGKV-IDQSTLEKCNRSEATwgrvpsDPFTGVAFTpHSQPLPHPSLKARIDHFL 332
Cdd:COG5113  846 EDMGDVPDEFLDPLMFTIMKDPVKLPTSRItIDRSTIKAHLLSDGT------DPFNRMPLT-LDDVTPNAELREKINRFY 918

                 ..
gi 389886556 333 LQ 334
Cdd:COG5113  919 KC 920
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
260-291 3.21e-04

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 38.70  E-value: 3.21e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 389886556 260 PEEFLDPITLEIMPCPMLLPSGKVIDQSTLEK 291
Cdd:cd16664    1 PEEFICPISLELMKDPVILATGQTYERAAIEK 32
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
263-313 3.96e-04

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 38.62  E-value: 3.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 389886556 263 FLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEatwgrvPSDPFTGVAFT 313
Cdd:cd23149    1 FTCPITSGFMEDPVITPSGFSYERSAIERWLETK------PEDPQTREPLT 45
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH