ID A0A161HMY3_9ASCO Unreviewed; 268 AA.
AC A0A161HMY3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE SubName: Full=Ubiquitin-protein ligase RMD5 {ECO:0000313|EMBL:ANB15367.1};
GN Name=RMD5 {ECO:0000313|EMBL:ANB15367.1};
GN ORFNames=AWJ20_2994 {ECO:0000313|EMBL:ANB15367.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB15367.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB15367.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB15367.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014503; ANB15367.1; -; Genomic_DNA.
DR RefSeq; XP_018737844.1; XM_018879979.1.
DR AlphaFoldDB; A0A161HMY3; -.
DR GeneID; 30034966; -.
DR KEGG; slb:AWJ20_2994; -.
DR OrthoDB; 208500at2759; -.
DR Proteomes; UP000189580; Chromosome b.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:UniProt.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16652; dRING_Rmd5p-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12170:SF3; GH10162P; 1.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:ANB15367.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189580};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 30..88
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 210..254
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 210..254
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 268 AA; 30469 MW; C228CC3413ECE42C CRC64;
MYLTRSGEFD VASTFMKETG VSVPEHLLGE FCKMYDILQH IQARDLAPAI EWATLKRSDL
LARGSNLEFS LHRLQYIDYL IEQNDSVKAI NYARRHLSAF KDRYFKETSQ LMSALLYVGT
IDKSPYASVV KFPTYEQLNM MFASEFCSLL GFPPQSPLYL AVTAGSIAIP TLSKMESVMK
RRGAEWTTTQ ELPVTIDLPE ILQFHSIFVC PVSKEQTTET NPPMMLPCGH ILANDSVRSL
GKESPTHMFK CPYCPVDTNY SQAKRVYF
//
