ID S9X6P9_SCHCR Unreviewed; 682 AA.
AC S9X6P9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Ubiquitin-protein ligase E3 {ECO:0000313|EMBL:EPY49441.1};
GN ORFNames=SPOG_01328 {ECO:0000313|EMBL:EPY49441.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY49441.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY49441.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KE546995; EPY49441.1; -; Genomic_DNA.
DR RefSeq; XP_013025470.1; XM_013170016.1.
DR AlphaFoldDB; S9X6P9; -.
DR STRING; 653667.S9X6P9; -.
DR EnsemblFungi; EPY49441; EPY49441; SPOG_01328.
DR GeneID; 25035657; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_1_0_1; -.
DR OMA; MLTPCHH; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0032933; P:SREBP signaling pathway; IEA:EnsemblFungi.
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:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 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:EPY49441.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..682
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004560303"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..676
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 417..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 77913 MW; 029C5A7194E3FD52 CRC64;
MDRRRWRPSA PVVILLLLFI FFAPVRRIPS RNGDSTEKSL QAERNWYSKI QNSTFLDAPE
IVRQSTTFPK EVLSKRNAIY KSSAGPGDSH SNHTSVVIGN WKKVSFDSFG KVSPNVTWHR
TLQNIVNSEK GGFSANVYEY PAQNSNDFTF VMNMENSNGT SLYQLVFYGD RIDKAHALLG
ATEVSPEFPG VDGIPWLFHE PADKSDLPFD GQEYFEVLKN KSLGRIDDRI DQISRGGWSP
LLYGEESVSC RAYFYGFNKN TGLSRKTLAA IEDEYYHPQG VSIKKMPDVL LSGLIYSPDC
NVAFTFSNYK GPRNFVFDAG LVRFASFYII IIFYQIFLLL RQMRLNSPSY VQRLSFITIA
IQACLDAFIA IFFLSINVVI ERGYLPFVSV AFLSLIPSVM FTMRYLALIL RVQNSNSPPP
PPLPPTPNNN ESTIEGEGEH GNANTTNVEN VQPEAGMTQH ERDQRDWSAV CLRFYFVILV
VCIVSLYSAF WPVTYRFYFI SILLFTCYSF WVPQIIQNVK QGTSRSFSWI YIIGLSISRM
YMPTFIFIYS ETTLKFPPKY TFAVALGLWM CLQVFILFAQ DTLGPRFFLP KRLFPSSSTY
DYHPIIQAGD LEALMHDANV CPICMQTIEL VSSGSTLNPA SRIVRRNYML TPCHHLYHRQ
CLLQWMETRS ICPVCRCHLP PV
//
