ID V5EVG1_KALBG Unreviewed; 598 AA.
AC V5EVG1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PSEUBRA_SCAF10g05417 {ECO:0000313|EMBL:EST09465.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09465.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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};
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DR EMBL; KI545852; EST09465.1; -; Genomic_DNA.
DR RefSeq; XP_016294454.1; XM_016433987.1.
DR AlphaFoldDB; V5EVG1; -.
DR STRING; 1365824.V5EVG1; -.
DR GeneID; 27416583; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_002173_9_4_1; -.
DR OMA; RTTYQPN; -.
DR OrthoDB; 164548at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 263..598
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 47..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 565
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 598 AA; 68243 MW; 9B2922FD42285597 CRC64;
MTDPFDPYSL TRVIALDSTG APLRAEARAM QRELGVDPTP EMIRTFMSMP YPGDPRADFR
HSSSSRSRPS DQTHLEKQKK RREEDEAKLA KIYESFEFDP LWSKLSDVLS RMKNDPGAAQ
ILLPLIESMM VVSQHVTSPD GETPIVPGDV RPPFSRSSTL GAHSRSSTQG PKTAKEIMED
NFFAFTEKHR KILNIMVRQN PTLMSGSFAL LVRNPKVLDF DNKKNYFTQQ LHKGRRDHYT
PLSLSVRRNS VFEDSFRYFS RKSGPEVKHG KLNVRFNNEE GIDAGGVTRE WFQVLARAMF
NPDYALFQPC AADRTTYQPN RMSYVNPDHL SFFKFVGRII GKAIYDGRLL DAYFTRSFYK
HILGKPVDYR DLESIDPEYF KSLEWMLNND ITDILDLTFS VDDEEFGETK IVELQPNGAS
IAVTEANKQE YVRLVTEQRL TKSIKSQIEA FLGGFNEIIP SDLIRIFSEQ ELELLISGLP
DIDVDAWKNN TELHGYSSGD AVIQWWWRAV RSFDQTEKAK LLQFITGTSK VPLEGFAHLQ
GVQGTQRFNI HKAYGADRLP AAHTCFNQLD LPQYESYEKL RSSLLLAMNE GGEGFGFA
//