Conserved Protein Domain Family
dRing_Rmd5p_like

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cd16652: dRing_Rmd5p_like 
Degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear division protein 5 (Rmd5p) and similar proteins
Rmd5p, also known as glucose-induced degradation protein 2 (Gid2) or sporulation protein RMD5, is an E3 ubiquitin ligase containing a Lissencephaly type-1-like homology motif (LisH), a C-terminal to LisH motif (CTLH) domain, and a degenerated RING finger that is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. It forms the heterodimeric E3 ligase unit of the glucose induced degradation deficient (GID) complex with Gid9 (also known as Fyv10), which has a degenerated RING finger as well. The GID complex triggers polyubiquitylation and subsequent proteasomal degradation of the gluconeogenic enzymes fructose-1, 6-bisphosphate by fructose-1, 6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK), and cytoplasmic malate dehydrogenase (c-MDH). Moreover, Rmd5p can form the GID complex with the other six Gid proteins, including Gid1/Vid30, Gid4/Vid24, Gid5/Vid28, Gid7, Gid8, and Gid9/Fyv10. The GID complex in which the seven Gid proteins reside functions as a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism.
Statistics
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PSSM-Id: 319566
View PSSM: cd16652
Aligned: 35 rows
Threshold Bit Score: 83.4574
Threshold Setting Gi: 167536837
Created: 23-Dec-2011
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
degenerated
Feature 1:degenerated RING finger [structural motif]
Evidence:
  • Comment:The degenerated RING finger is characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
Feature 1          #  #                    # #  #  #                     #  #   
gi 29840869  336 FACPILRqQTSDSNPP------IKLICGHVISRDALNKLin----------ggKLKCPYCPME 382
gi 74621927  276 FICPVLKtLCVDENIP------VMLECGHVISLEAASVLsqeg-------vlnSFKCPYCPEM 325
gi 74965980  345 FTCPILKeQCDAENPP------MRLICGHVISKDAINRLttsirqqrnssrlsKFKCPYCPRE 401
gi 360043114 417 FHCPVIKeVISESNDGasgggpVRLTCGHAISRDAFNSLasg--------dksRMKCPYCPVE 471
gi 405947210 194 FACPILRqQSTEVNPP------MRLICGHVISRDALGKLsn----------nnKVKCPYCPVE 240
gi 390363119 334 FACPILRqQASENNPP------MRLACGHAISRDSLNKLin----------gsKIKCPYCPVE 380
gi 761906437 182 FTCPILRqQTSESNPP------VRLNCGHAISRDAMKKLvgh---------sgRLKCPYCPLE 229
gi 221112644 331 FACPILRqQCGQSNPP------MRLVCGHVISKDATQRLth----------gnKLKCPYCPVE 377
gi 313244345 247 FSCPILReQTTLENPP------MRLICGHVISKDARDKLasnsh-----tqgkIIKCPYCPTE 298
gi 919068809 334 FACPILRqQSNDSNPP------SRLICGHVISRDALNKLan----------anKVKCPYCPVE 380

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