Q6FQK7 (UBC6_CANGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 6
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein UBC6
Ubiquitin-protein ligase UBC6

Gene names

Name:	UBC6
Ordered Locus Names:	CAGL0I05478g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces › Candida glabrata

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains By similarity.
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Endoplasmic reticulum membrane By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	Ubiquitin-conjugating enzyme E2 6		PRO_0000082548
Regions
	Topological domain	1 – 224	224	Cytoplasmic Potential
	Transmembrane	225 – 245	21	Helical; Potential
Sites
	Active site	87	1	Glycyl thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FQK7 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 0A7EC968C091001A	FASTA	246	28,400
	10 20 30 40 50 60 MATKQAQKRL TKEYKMMVEN PPPFIIARPN EENILEWHYV ISGPPDTPYD GGQYHGTLTF 70 80 90 100 110 120 PSDYPYKPPA IRMITPNGRF KENTRLCLSM SDYHPDTWNP GWSVATILNG LLSFMTGDES 130 140 150 160 170 180 TTGSITTTQQ EKKILAKKSM YYNTFNSTRF KLVFPEIVEK NITELQRRKQ EEKDMSMFEK 190 200 210 220 230 240 KEDPLVKAAR EKAIEVKDIV NPEDRIRAEQ ALKELEKQHN DKPNGSSSMF YIGVALFLFL VGLFMK

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380955 Genomic DNA. Translation: CAG60424.1.
RefSeq	XP_447487.1. XM_447487.1.
3D structure databases
ProteinModelPortal	Q6FQK7.
SMR	Q6FQK7. Positions 5-160.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2889269.
KEGG	cgr:CAGL0I05478g.
Phylogenomic databases
KO	K04554.
OMA	SFMTGDE.
OrthoDB	EOG441TMP.
Enzyme and pathway databases
UniPathway	UPA00143.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UBC6_CANGA

Accession

Primary (citable) accession number: Q6FQK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program