YDE1_SCHPO
ID YDE1_SCHPO Reviewed; 1647 AA.
AC Q10435; O14101;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable ubiquitin fusion degradation protein C12B10.01c;
DE AltName: Full=HECT-type E3 ubiquitin transferase C12B10.01c;
DE EC=2.3.2.26;
GN ORFNames=SPAC12B10.01c, SPAC31F12.02c, SPAC637.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.
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=2.3.2.26;
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA22594.1; -; Genomic_DNA.
DR PIR; T37568; T37568.
DR PIR; T38617; T38617.
DR RefSeq; NP_594633.2; NM_001020061.2.
DR AlphaFoldDB; Q10435; -.
DR SMR; Q10435; -.
DR BioGRID; 278072; 51.
DR STRING; 4896.SPAC12B10.01c.1; -.
DR iPTMnet; Q10435; -.
DR MaxQB; Q10435; -.
DR PaxDb; Q10435; -.
DR PRIDE; Q10435; -.
DR EnsemblFungi; SPAC12B10.01c.1; SPAC12B10.01c.1:pep; SPAC12B10.01c.
DR GeneID; 2541575; -.
DR KEGG; spo:SPAC12B10.01c; -.
DR PomBase; SPAC12B10.01c; -.
DR VEuPathDB; FungiDB:SPAC12B10.01c; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_1_1; -.
DR InParanoid; Q10435; -.
DR OMA; FFTIHAQ; -.
DR PhylomeDB; Q10435; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q10435; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; PTHR45670; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1647
FT /note="Probable ubiquitin fusion degradation protein
FT C12B10.01c"
FT /id="PRO_0000194999"
FT DOMAIN 1294..1647
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 192..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1257
FT /note="K-box"
FT COMPBIAS 192..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1614
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1647 AA; 185617 MW; A2A005E7DFB0676B CRC64;
MSVQAYTNTP NLPNLIHSES ITNSPVFIPN LRSKSDNKHR LNTSEELPFT KKRRATKHFL
KMEVSAKISE PPSSKSVEFG RHLNMRHDFS ELLEQPLTTS KTRVFKSFNE KLKGKPQLVK
SDKGVLPLNK QSDILNSYER VLSNASVDSA LDKKAEVDII PFDKSVMEPK NITFNDKSGL
TKFGNSNSYE TTYSDSSNYH TSTDSSQYND QDDHVYDDTN DGTDDDINNN EYKDDESSSG
SESYERDEDV DEEEEEDDDE NNDEGDDEDE NENDELRSEN GSPNPSAAVI NEQENMNMSG
IEEYDETNLL NELGRIRRGN QFQSLASSIL SSGNLENSDD EDVSLGPQTY RFNSSFHPFR
SAFSAPGVQF GRLLEGIKDF SDPTVQMLSL QELSEAFAMS TEDMLVGLFS TDSYIAAFSE
ILSGRNYDFG EVSIQLMLSC TTCVSNMMEA LPLCMAKIAY SPIVRILCER MFDMQYIDIA
EQALGVLERL SKDFGICILE HRGMLAALQY FDFFYTTVQR TAISLAANCC KFLDESNASA
AEEIIPLLSN ILQSSDTIVV SKAYSCLETI IESLKTSPNI IETIISEDLI TTIVNALTNS
TSQNKSMHLQ VQLLHIISSL CQSSSALILP FLNHNLPDVM YEMLCGIPPS DTSHQADMIT
MQSLYYCPIE LIENLLRAIT SLLPKNTSNL SDEFNTKLYR LNSILLTVVM DIYFIVPLHD
IRSLAVTTAL KMLCSIRENN LDGLVCSLPL SSFIASILNS RKSDNFLKRD ALEMCLFLLE
ALPNVYSSLF IREGVVQEVG FLVRSTNADM KKIKLSISFS QNKSAARHEE LKNLSTLKSL
AKEFLSNYKE ENLENSTLVQ LKQLSKHLLS ETKQDESFSE LAKIFQEGSN ITSHELLHSG
LIHNLLLSLK KFGSSSLRTF LLAMNTCDER EVLEFGNGPL VSLIFCLQNL LSTVENFQLS
TLPPDTENAV DHVFSRQFKL RLMALPGSRI RPPFRSLVVS INGLATIRTL DNYLHSRISV
RNETGRRFSI LREAGSLRES MSGSSRNSSG DYTDSMSQDA PNHTTEPSER RDSSTSSHFE
EHFVFSLMGK KVPRNKTIFR ILYEYIQLSD DHTLDDFWKT PVPIFYGEPD CIHNDMKGEL
NYENETEGFS INIREILDLL SILYYGIRDV HTLFPDKHFR GNIENILTDF SNWKLSAKLN
RQLEEQQLVV HGCLPSWCIS LTSAYPFLVP FETRYLLLQS TAFGLSRSVS FLLSRNPELS
KNESSSILQF VSLHRQKIRI SRKKIFNYAL HLLATYAASE NILEIEYEDE VGSGLGPTLE
FYTSVSKEFT LNSLDIWRND QPNSKFVYQA SGLFPSPIPL LGSSPENERK ISLFFALGQF
VARSIYDSRI ISIQFNPLFF ARNIPLTISS VAKVDKGLAN SLRYLEKLIP GKNPTNAETD
IKLEDLHLDF TLPGFPSIEL IPDGASTPVT TFNVSDYLNY VIDYTVGKGV QQQLEAFQNG
FSSVFPYTSL QVLTEHELVT LFGTVDEDWS YATLMKSIVA DHGYTMESPT IQRLLTLMSQ
MNFQEQRDFL QFITGSRKLP IGGFAGLNPP LTVVRRLNEP PYVPDDYLPS VMTCVNYLKL
PEYSSSEVLG SRLSKAILEG QGSFHLS
