GenomeNet

Database: UniProt
Entry: R1GMB7_BOTPV
LinkDB: R1GMB7_BOTPV
Original site: R1GMB7_BOTPV 
ID   R1GMB7_BOTPV            Unreviewed;       753 AA.
AC   R1GMB7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative ubiquitin-protein ligase e3a protein {ECO:0000313|EMBL:EOD47139.1};
GN   ORFNames=UCRNP2_6112 {ECO:0000313|EMBL:EOD47139.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD47139.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB916359; EOD47139.1; -; Genomic_DNA.
DR   RefSeq; XP_007585380.1; XM_007585318.1.
DR   AlphaFoldDB; R1GMB7; -.
DR   STRING; 1287680.R1GMB7; -.
DR   KEGG; npa:UCRNP2_6112; -.
DR   eggNOG; KOG0941; Eukaryota.
DR   HOGENOM; CLU_369600_0_0_1; -.
DR   OMA; ININMDA; -.
DR   OrthoDB; 1820836at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
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; 2.
DR   InterPro; IPR015158; Bud22_dom.
DR   InterPro; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   Pfam; PF09073; BUD22; 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   Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:EOD47139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..293
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          274..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          360..392
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        274..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..671
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  83064 MW;  465F92E860317415 CRC64;
     MGKLEGEQGV DQGGVAQEFF RVALAEAFNP DNGMFTVDSQ TRMTWFQPFS LEPLSRFELI
     GLLFSIAVYN GITLPSVRII SEKGGQTFRG YEFSFEARGL IININMDAMN EDAEIPSPHT
     LLDYTDGLEI SPSSSNPTPI VNWPPGPEAP LVTNTNREQF VRDYVSWLTD KSIRPQFEAF
     ARGFRTCLPA QHLALLRPSL LSHIVEGSTD IDTRALERVA RYDGGFDAAH PFVRIFWDSV
     HAMPQEQKRK LLEFVTASDR VPVAGIESVV FWHASSNSSP PRPSTTRSSY LPTRERADPH
     GHATAAATTT MPKRKRSDDS EQPAASDRAT AKQRKHLPPR LEQGKKALNK ALRVSRGFER
     QKLSRRRKAA EKEGKAKEVE RIDAEIEALK KVEYHVLAET HLYKTLLKIK SVAEHPALPP
     WVKVPEGKGK GDAAAMNVQA RLFNANPTKE AMGEVVRDVR AILGLEDGGK GPKAKKAKGG
     EEKAGKAKAR VATPESSEES SDEESMDDGE EGEWDSEEFE GFSERIAASS DEESEEDIKA
     ALKRNYKPVR DLSFTPPSSR EASPSLSPEP TFSDDSVSES SESAPKSKSK AKGPVITNKS
     TFLPSLSAVG YISGSESEAE DLDEDIAPPK KNRRGQRARQ QLWEKKYGKE AKHLGKQKEK
     EKNDRNAGWD AKRGAVDGAG GRGKGRFGRS DRGENRGGRG PKATDANLVE LGKKKDHRDD
     AGKLHPSWEA AKKAKEKAKL GNVQFQGKKV VFD
//
DBGET integrated database retrieval system