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Database: UniProt
Entry: C5DWC9_ZYGRC
LinkDB: C5DWC9_ZYGRC
Original site: C5DWC9_ZYGRC 
ID   C5DWC9_ZYGRC            Unreviewed;      3277 AA.
AC   C5DWC9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   OrderedLocusNames=ZYRO0D13794g {ECO:0000313|EMBL:CAR28098.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28098.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034494}.
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DR   EMBL; CU928176; CAR28098.1; -; Genomic_DNA.
DR   RefSeq; XP_002497031.1; XM_002496986.1.
DR   STRING; 559307.C5DWC9; -.
DR   GeneID; 8204294; -.
DR   KEGG; zro:ZYRO0D13794g; -.
DR   HOGENOM; CLU_000215_0_1_1; -.
DR   InParanoid; C5DWC9; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008536; Chromosome D.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR   InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR025527; HUWE1/Rev1_UBM.
DR   PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF06012; DUF908; 1.
DR   Pfam; PF06025; DUF913; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF14377; UBM; 2.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          2941..3277
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1649..1670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1902..1930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1964..2028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2048..2086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2138..2160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2287..2318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2411..2453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1966..1983
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2048..2080
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2429..2453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3244
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   3277 AA;  375712 MW;  9CB63A9A9241FC77 CRC64;
     MVKLTRYERL QKEQSALSFK PLMDELTQCS EEEFVEKLKG IREWDRSRDD LFTWIPVLNR
     IDEMLTRVVE KYSYQSIDPK KQPVKLIEMT ADEEELCVNL SQFTSRLLCN TENRFIYSSL
     DVMNNLLNCP NFRVKLGATK VLAIMGERYV ITRERFDKDN ILGNPQLKRK LLRLALSIPS
     STMDEERGEH FSLVELFLDK KKYPSKWSKL KYTYYTAGGG NSSNNKRAPP SSSGKEAVQS
     SSMKRLVFSK EDLQSHSLQQ LFDKGMEVLP SDVWFDFSIQ VTMAKAFSDD SFENIELRKL
     LIRTKFIAIA VVNTVYVPPQ VSSKLFEVDP YAFNSLTDFV SLSETKIPKE LRLDSLFALE
     CTSLKHVWCS DIVRNLGGNM SHGLLFQILR YIGKILRDES QEVDEEYNVR FFYLISNLAD
     VKALHESLLG AGLIPSLLDI MLVKNTTYRR TLASATHLLE AVINDGDSTA EFIGNDGFAI
     LINSIMEEVD FALEHPEYGG PPKYSVVYYS VSFRQLAYIR SLLKLVLKLL KTDSGDRIRN
     LIDSPILISI KKILENRPVF GYTLITYALD IVQKVINSEP TIYPILVEAG LVPYIIDHFP
     EMMGPSSELL SILPDVISAL CLNSEGLKKA KENNMVRFLF DAVTNPEYAK ILIWKESATD
     LGASMDELAR HYPDLKPQIL QCFHDIVKEL PKRINFKQSY LYEPSNSKEL FFQSKDEPAE
     EKEENAGELA FWEVQEATPL VDCFADVIYG MSLDNSTLEN LPEKLNVRDL FSIIIMDRPP
     FDYTSSQAML NFTDVLQLFD EQKKDYVFPE MMKVLQERLQ HVSEFLNFNN EESYLLRARK
     DRDNSDIDGL LGEFSGLAAL LYLMTDVYVN VTSLIPARIH QILNYFDKNG FELIKLLRLL
     YQKCALEEMY LTQRMPDEVL TQTMPEPLGT ASPVQIHATK PVKQAQKDDF TSAKYKNTFE
     ARFLLNKLQS CTAMLFRCFL RLTHARNMEV EQEKQVVEVH VFDEVSYQMQ EMLQAVDLEK
     SLPYFLVIFN FINYIYSFPK TSITGTGILQ TVPAYLFYQY GGYRFYSDAI KTLFAKMSTF
     KDIAAIEEVD YIKNTDEVLT LSCLLNLLTF FNRSLSLDTM EHIPCMEVFG LVPKIGDDYV
     LTKALMDLVK KMSLCLVYKL ANEGCLFNSR ARTVPYPVFK QVLTMLKNTY TNINADEDSV
     LELNWDLMPP RYRVIDALKS CGLTEEQARK FITAEEHAYE SGGLNDDELF PSKPDVFSEE
     GWERYKSIKL SGSLSLTPME PRHGNDMFSS DRLETMTDEF LDNGLPQKVF DVLPFYPKLV
     NAIARTLLQM FSNYDEPVEN FASQVLEKIL QTNLEDGATL SSLIHIFGIF LNEKQVYENT
     GRLISEFLEY LQKSLSPEYI NSSWFSKALY VYEIILAKSE VPVMESLPDD IPVRYRLPPT
     PNVYRIPANI KQNIFDSLIR VGEITNFYSA LATCRILIFY ARDEGYASEI ARSGTLSKLL
     KVIGIFQKSD KINFLESSFL LLVRRCFETV DIVSTLIRCE LNKSFTTRVI GDHKEKERDL
     TSLIEEKPHV VMRNPDKFID NLCETARFQS FSGDGKLQEY NVHRNFDDKP SENEDVATKN
     EANSAVQNRT GIIHLLLSQL MAAYKKDWTS EPNQPNDVKD TSNDKQEKVD PTKNPVCAYM
     MFLLKVLIEL VSSYKQCKFE FLTFERRNQY TEFPKPKSTA LNFFLYQLLD KSTVHEQDKF
     EAKRREVISM LARSVVVGFI AAVQDDNNKK SDLKAIDPDM NFIRKFTIES IMRALKNSTM
     TSKLLEANVS KLETWFKVIS SMVLVQAPYL RLILDSNKLD ADQYQICKLM MDMNVPASVT
     ECIAGVDLNY PFAKNLFNNA VDPLNCINSI RNTFADLFKI ESNDDEEDVD EESDKEDPPD
     MFKNSALGMY DVEDIEEDDD DDVSLMGDDE DIAFVDGDDG EFEVVFSDDN EHGSGHDDHS
     DIGDSGDEEM DYSSDDHDME HMHDHEDHSE EGEDEEGSGE SYYSDDSNGD IEVIDVDADD
     GLEIELDDYD VDESDWESGL SELSASEEDL EDGEDGENED DANVGGLRRR WATSDGFDII
     EDTSDEDEAT GVFQGLEHVF HGEGQPLIRI QDARRHGRHH NHPFRRNHGH SLLGPPSLTL
     LNGGRRHQSN LINPLGPSGL EEIENGISDQ LVNVGNGARH RPEHTHFSNV LFSGEFFDER
     SPDGIILKPT VSRWKDIFDM FYDTKSYASF IIPTVIAKLY GPSLRLYREA EERREQEYNQ
     RLEKLREEET ERVHQTARPA SQPTAPAATS RDVEEGHEPH EPVYVTIDGT EVDIGGTDID
     PEFLNALPED MRSEVFAQHV RERRAEAMRN DVHSREIDSD FLDAIPESLR EEILEQESAE
     TRFSNIIHSI GEQTHEHDQD EDMLSDEGEI DDGNRPGEER RRSESDKKKP SRTYFSPLVD
     RAGIAAIMKS IFISQPYVQR EMYHELFYRL CSSKQSRNEI INMLLMILTE GIIDENSLEK
     VYNLISSRAN GSGKIQNSVS GGRQLPADCS PLIVANQAVE ILQNLLDSDN RLKYFFITEH
     ENLMVNKAPV KNKKDIFHKN LKWPIKYLFG LLDRRIITDE SVLMDLLTRI LQVCTKPINA
     LSKNSDESSG SKKKFQVPYF DRKDFERIVS IINMDSCNTR VFQQTLSVMH HLSMLKDAVK
     IFTEELISLA LKTVRNLVAD LNKLTEESSM VSNGTEFNSE LVQKFTMPSS DQAKLLKVLT
     AVDYLYTHKK DLSEEDVSKL MGVYNEMQLG QIWSSLSKCL FEFENRKGLN TSATVLLPLI
     ESLMVVFKHI KTSQSGNKNT ALKYEDEKKL DFSNSGTESF FFKFTEAHKK LLNQMIRSNP
     KLMSGPFSLL VKNPKVLDFD NKRYYFNAKL RSDAPDRPKL SISVRREQVF LDSYRALFFK
     SNEDIKKSKL EITFKGESGV DAGGLTREWY QVLSRQMFNP DYALYLPVES DRTTFRPNRT
     SGINPEHLSF FKFVGMVIGK AICDQCFLDC HFSREVYKNI LGRPVSLKDM ESLDLDYYKS
     LIWILENDIT DIIEETFSLE TDDYGERKVV ELIPNGSEIQ VTEENKQEYV KKIVEYKLHL
     SVKEQMDNFL QGFYALIPRD LISIFDEQEL ELLISGLPDV DVDDWRNNTN YVNYTANCKQ
     INYFWRAVRS FDAEERAKLL QFVTGTSKVP LNGFKELTGV SGICKFSIHR DYCPTDRLPS
     SHTCFNQLNL PSYNSYDTLR GSLLLAINEG HEGFGIA
//
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