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Conserved domains on  [gi|42573231|ref|NP_974712|]
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RING/U-box superfamily protein [Arabidopsis thaliana]

Protein Classification

RING finger protein( domain architecture ID 10614451)

RING finger protein may function as an E3 ubiquitin protein ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Ontology:  GO:0016567|GO:0061630|GO:0008270
PubMed:  19489725|11007473|22154517
SCOP:  3000160

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-RING_2 pfam13639
Ring finger domain;
289-318 4.76e-04

Ring finger domain;


:

Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 37.77  E-value: 4.76e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 42573231   289 ILACGHVYHGECLEQMTpeidKFDPSCPIC 318
Cdd:pfam13639  18 VLPCGHHFHRECLDKWL----RSSNTCPLC 43
 
Name Accession Description Interval E-value
zf-RING_2 pfam13639
Ring finger domain;
289-318 4.76e-04

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 37.77  E-value: 4.76e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 42573231   289 ILACGHVYHGECLEQMTpeidKFDPSCPIC 318
Cdd:pfam13639  18 VLPCGHHFHRECLDKWL----RSSNTCPLC 43
RING-H2_Vps cd16484
RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, ...
 259-318 8.83e-04

RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, Vps18, Vps41, and similar proteins; This subfamily corresponds to a group of vacuolar protein sorting-associated proteins containing a C-terminal C3H2C3-type RING-H2 finger, which includes Vps8, Vps11, Vps18, and Vps41. Vps11 and Vps18 associate with Vps16 and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form.


Pssm-ID: 438147  Cd Length: 48  Bit Score: 37.10  E-value: 8.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573231 259 TCGACSRPLSEKslwssqkifmTNELSVSAIL-ACGHVYHGECLEQMTPEidkfDPSCPIC 318
Cdd:cd16484   1 KCPICTLPLKES----------DVGANSPVVVfFCGHMFHKFCLPELSMT----EAACPIC 47
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 289-318 1.50e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 36.33  E-value: 1.50e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 42573231    289 ILACGHVYHGECLEQMtpeIDKFDPSCPIC 318
Cdd:smart00184  14 ILPCGHTFCRSCIRKW---LESGNNTCPIC 40
 
Name Accession Description Interval E-value
zf-RING_2 pfam13639
Ring finger domain;
289-318 4.76e-04

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 37.77  E-value: 4.76e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 42573231   289 ILACGHVYHGECLEQMTpeidKFDPSCPIC 318
Cdd:pfam13639  18 VLPCGHHFHRECLDKWL----RSSNTCPLC 43
RING-H2_Vps cd16484
RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, ...
 259-318 8.83e-04

RING finger, H2 subclass, found in vacuolar protein sorting-associated proteins Vps8, Vps11, Vps18, Vps41, and similar proteins; This subfamily corresponds to a group of vacuolar protein sorting-associated proteins containing a C-terminal C3H2C3-type RING-H2 finger, which includes Vps8, Vps11, Vps18, and Vps41. Vps11 and Vps18 associate with Vps16 and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form.


Pssm-ID: 438147  Cd Length: 48  Bit Score: 37.10  E-value: 8.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573231 259 TCGACSRPLSEKslwssqkifmTNELSVSAIL-ACGHVYHGECLEQMTPEidkfDPSCPIC 318
Cdd:cd16484   1 KCPICTLPLKES----------DVGANSPVVVfFCGHMFHKFCLPELSMT----EAACPIC 47
zf-RING_5 pfam14634
zinc-RING finger domain;
260-318 1.32e-03

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 36.25  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 42573231   260 CGACSRPLSEKslwssQKIFMTNelsvsailaCGHVYHGECLEQMTPEIdkfdpSCPIC 318
Cdd:pfam14634   2 CNKCFKELSKT-----RPFYLTS---------CGHIFCEECLTRLLQER-----QCPIC 41
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 289-318 1.50e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 36.33  E-value: 1.50e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 42573231    289 ILACGHVYHGECLEQMtpeIDKFDPSCPIC 318
Cdd:smart00184  14 ILPCGHTFCRSCIRKW---LESGNNTCPIC 40
RING-H2_RNF24-like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
 288-321 1.68e-03

RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; This subfamily includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438132 [Multi-domain]  Cd Length: 47  Bit Score: 36.21  E-value: 1.68e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 42573231 288 AILACGHVYHGECLEQMTpeidKFDPSCPICTMG 321
Cdd:cd16469  17 GVCPCGHAFHTKCLKKWL----EVRNSCPICKSP 46
RING-H2_RNF32 cd16471
RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 ...
 283-318 5.06e-03

RING finger, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, proteins with double RING-H2 fingers may act as scaffolds for binding several proteins that function in the same pathway.


Pssm-ID: 438134 [Multi-domain]  Cd Length: 46  Bit Score: 34.91  E-value: 5.06e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 42573231 283 ELSVSAILACGHVYHGECLEQMTPEIDKFDPSCPIC 318
Cdd:cd16471  10 KGRKCTLLSCSHVFHEACLSAFEKFIESKNQKCPLC 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.
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