ID   A0A2D3UWC5_9PEZI        Unreviewed;      1232 AA.
AC   A0A2D3UWC5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Related to ubiquitin-protein ligase E3A {ECO:0000313|EMBL:CZT21071.1};
GN   ORFNames=RCC_06932 {ECO:0000313|EMBL:CZT21071.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT21071.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT21071.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT21071.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FJUY01000010; CZT21071.1; -; Genomic_DNA.
DR   STRING; 112498.A0A2D3UWC5; -.
DR   OrthoDB; 5471864at2759; -.
DR   Proteomes; UP000225277; 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   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; 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; 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   Ligase {ECO:0000313|EMBL:CZT21071.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225277};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          864..1232
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..326
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1200
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1232 AA;  137041 MW;  0C38774A34FEE1E8 CRC64;
     MPPPSSWSSR LLSSGSASSN ARDKPLPRAP SDYLDTPTLN HDRRPPSPTR PRTVGPRQHA
     HNRSASNPLP KIFGRKKSTN FHDTHGTGGE GLVRVSESVE PAPSGVISSK RGKAVDDGSK
     TTRKCMCCDS RVNVPRELPR FRCLCCLTIN DLKPVEEQTE DDQGRPILKT LPGQLSSSNH
     SPLSIERTRA IIDRCLDVYL EERCRREEPN APDPTASISE DVFGSEQRSA AMPIRPRNGK
     QPLDSSASLS RSPPESSGDL FSTSATIREF GEFDLFAGTR METPPLVQKL STSAPTHDTV
     SPARRKPVPT PSKPIRKPPP PPLNASNRRP SHHRVHIHGN LAPDGLHSPG PTASPKLTPG
     EMEHRRHQDR IKAIFRPLED YIVATVGDFH CLNSSFSTLR PVASGRTRSE SNIVTPPPEP
     HDVFQPSPME GLSGLDAKTL LIGDIGENGS WWTGKVDRNR SEIRRKKVGE GPKKTVSSRS
     ANINWAELTS WYGLVHTAGE DWQKNLENLK LSKFQLPTEN VAGDVNTEDI EEELGSAREH
     AVRTLLKVTE NLLKRPSRPI KEPGDLRFLL ILLSNPSLYP SSASSQTTLP SRRSNGHAQA
     SPRKSPARDG TQHNGLLKRI FGLMAHSTDA CHRYLVGWFT RFDEHHLVKT IDLVASFVTY
     RIARTSGRPR RKSLVNDGGL IPDLSGSTMN TSAQLHSAMG LGGSVKKSAV DPNAEPDWVG
     DWQIKAAAKV MSLLFAANNV WQGKRRDXDK SSMTKPRKPG QLLHTSSFYN TLLDYQDLIA
     DFRVWETRRD KFAFCQYPLF LSMGAKIKIL EHDARRQMEI KAREAYFDQV IRQRAIDGHF
     TLRIRRECMV DDSLRQISAA VGAGQEELKK GLRVQFTGEE GVDAGGPRKE WFLMLVRDIF
     DPNHGMFSYD DDSNTCYFNP NSFETSDQYY LVGALLGLAI YNSTILDVAL PPFAFRKLLA
     AAPSSVTSAS NVSTMTGTKG QMSYNLEDLA EFRPSLAAGL QQLLDFEGDV EATYCRDFVI
     PVERYGVITN VPLVTNGESI PVTNANRQEF VDAYVRYLLD VAVARQFEPF KRGFFTVCAG
     NALSLFRAEE IELLVRGSDE ALDVDSLRAV AVYENWRQVA EPHHLHPNPA KSVPVIGWFW
     ESFAEASPEK QRKLLTFITG TDRIPAVGAT SLVLRIVAGG DGWGGGLHDE RQRFPIARTC
     FNMLMLWRYD SREQLETKLW RAVDESEGFG LK
//