ID A5DQL6_PICGU Unreviewed; 536 AA.
AC A5DQL6;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PGUG_05567 {ECO:0000313|EMBL:EDK41469.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK41469.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK41469.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- SIMILARITY: Belongs to the HRD1 family.
CC {ECO:0000256|ARBA:ARBA00010089}.
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DR EMBL; CH408161; EDK41469.2; -; Genomic_DNA.
DR RefSeq; XP_001482547.1; XM_001482497.1.
DR AlphaFoldDB; A5DQL6; -.
DR STRING; 294746.A5DQL6; -.
DR GeneID; 5124506; -.
DR KEGG; pgu:PGUG_05567; -.
DR VEuPathDB; FungiDB:PGUG_05567; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_497911_0_0_1; -.
DR InParanoid; A5DQL6; -.
DR OMA; KLKCGHI; -.
DR OrthoDB; 2912447at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd16479; RING-H2_synoviolin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR22763:SF184; E3 UBIQUITIN-PROTEIN LIGASE HRD1; 1.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..390
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 400..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 60710 MW; 7E73F17B52A06395 CRC64;
MTLTSGAKYF IGYSALSVAL LAWSIASSLE VSHNYFSFIV KITDGFKLGI LINFIFFSFI
ITARALQLLL FGELRIIEIE HIVESVPMFT VNLLFNLVTN DHNLLNCVLL GFIVMSKLLH
VILTDRLDFV HMKVVNTLAE ERYTSSDVLR RYISSLYTWL IAFFIVADFV FAKFLVYDAF
KGINSVTCLL FGFQFALLGV EALTFFSKLL LNIYELAVYN DANEDDDEFD VDADDTISEV
DSGSRVWEKK GYYNKAIDIF SSSLKAVSYL AFIYLLTFHS GLSLPISMLQ GTYSSIKKTY
VEITSLFAFI ESARRLDSQL ATATTEDLSA TDNLCIICRE DMYSVEAYRE TRGRPLPARK
YPKKLDCGHI LHMGCLKDWL ERSENCPLCR RKVFAGNPTS ITDTNATNAQ PEQPIPQHPI
AHPEEVLDRR LEEYTELARQ QNLAREQAAS SSNRQEGQAS GIQEAGDNSD QLQTIKLPDN
AIIPPNWTIL PIHRMSEMQY GVDFSTRHRG TLSIRPSVGG RELDILRPRR SESENE
//
