ID B3LR52_YEAS1 Unreviewed; 758 AA.
AC B3LR52;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Transmembrane ubiquitin ligase 1 {ECO:0000313|EMBL:EDV13055.1};
GN ORFNames=SCRG_03984 {ECO:0000313|EMBL:EDV13055.1};
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV13055.1, ECO:0000313|Proteomes:UP000008335};
RN [1] {ECO:0000313|Proteomes:UP000008335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; CH408051; EDV13055.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LR52; -.
DR HOGENOM; CLU_010475_1_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase 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; cd23117; RING-H2_TUL1-like; 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; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF162; RING-TYPE DOMAIN-CONTAINING 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 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EDV13055.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:EDV13055.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..758
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002791322"
FT TRANSMEM 400..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 699..752
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 758 AA; 87852 MW; C8AA61E994F96632 CRC64;
MEIDGNTLVF IIVILFLFFS SPGGDGVSSQ YEFNQLQRLK QQFRTEHNTF VNMTYTDSFR
NITGLKLSYQ DMLNNPLQNA TYPLPGKDYD RWFPNQNYMV LPNDVIEAIN TEVWNTSNDD
ASNLFPPNIT STLLGKIDLV SNNKYEKIRM PVPRFYEPAT DFSEDIPPEG ETYWSEWPSY
GELHNVSFQH GEIAIQISHM SNLQDNNNYL RRNFINKKND RWKLLNLQID FSDKAEKEKH
SIYSKAVYDI QRGRILSISQ SSKFHSLFAL PHYMSFQNDY NEKIFNDVKE LVDEFWNFTD
YTDVMTMKDV QDAYNNANFK CEYLIFLQLE PWNQYTRDQI KLIDDELNWP LGRPANLSSL
PPINVVSGLL YSPDCGVRLG LHNVKGTRYE LKIMSIRKHL LFGIALFAAQ IYLLLTQMHH
TNTPSMVNKI SFYCFSMINL VDGSLATLYF VAASVVPELY LPLVISAFSC FILASIFEIR
YLISIYASQV NEQNVGIINL LRGNTGTYDE NRPRPAFIPD EGSIGGSLYG RFFFMLIIFT
FLILSSTSWP RQLRMVFEYI LIFILNSYWI PQIFRNAVKG IPSRRERARS SIGGNRSQNK
MPLLWSFVIG TTIIRSLPVV YVFTYSSNVF RHHKDVHFVV FLSLWLLFQI SILYSQDVLG
SRWFLPKHTI PDGYSYFKPL SNEYISEHGG GTAEHTVDCA ICMSDVPIYI EEIPETHKVD
QHSYMVTPCN HVFHTSCLEN WMSYKLQCPV CRSPLPPL
//