ID   A0A2A9LZE3_9APIC        Unreviewed;      1697 AA.
AC   A0A2A9LZE3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=BESB_030190 {ECO:0000313|EMBL:PFH31145.1};
OS   Besnoitia besnoiti.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX   NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH31145.1, ECO:0000313|Proteomes:UP000224006};
RN   [1] {ECO:0000313|EMBL:PFH31145.1, ECO:0000313|Proteomes:UP000224006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH31145.1,
RC   ECO:0000313|Proteomes:UP000224006};
RA   Schares G., Venepally P., Lorenzi H.A.;
RT   "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PFH31145.1}.
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DR   EMBL; NWUJ01000016; PFH31145.1; -; Genomic_DNA.
DR   STRING; 94643.A0A2A9LZE3; -.
DR   VEuPathDB; ToxoDB:BESB_030190; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000224006; Chromosome xiii.
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; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   PANTHER; PTHR45700:SF2; 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   Reference proteome {ECO:0000313|Proteomes:UP000224006};
KW   Transferase {ECO:0000313|EMBL:PFH31145.1};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1362..1697
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1665
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1697 AA;  181218 MW;  F630DE3DB0C1A1B5 CRC64;
     MFADFRHNSH RTIDLSGSSR PSFVRGRQSG LSTGAGAVSR SSLLEFQRRE RQLREQHRKS
     VDASSKIQKC WKAAFARRRA KAESRRAFDA TVAALYRGEA AGSDAQTAEE SSAASGQTGG
     REARRAGPGG CPRCRAEIRR ALPVLIRNLA FFFDPEDDGS RKISQACLRG AEEKEASAGA
     CGSDADQGRP ETAVVRTREE TRAHAPVHGG EEGADLAEGT LFHFRGAPGC ADDVSRLGLV
     CEWLRELGKH HESGGGSCGE GKERWGHDPT ALAKNGSLAA TEVEPSCLFC LAVSQPSRRE
     NGVSSAPAPL ALSTPCAAVA LPPADAPAGR PSDPPGPSSW GLQGGAPPCV RVSPRLTALT
     LLRLVLQCVA LRYRATLFES APASLLPPLR FRGGSDAPAR IGSSSGAFAW TQLRPALGWR
     GSVLSSSLSA LARAQAAPAG SERQAAEGER AEPARFTALG SEAPKQPEGD RSPFSRAGEL
     AQGGLRQAEG LSEARGGDAG ARGAPALTPA PFLLLPPERS LAERQYLQSE REVNSHEAGL
     WVQIARDVLL ALSAAPLAAG ASLAGGASAG DADAARTDAS DAAGSEPEAV ASRSCAPARA
     CHGEEALADL VKNWRRAGRH GMMALLADAL VGALLASGIA SAGEEGSARQ QFEAVERAER
     QTARVVETCL RACDPNDVGG EVEFLVHLLG APCLLPVPSG AGAAEAGPWR RRVGLLSRLV
     EGRLASVPGT SALQANLVAM QVQGVAAKLR KAEGAEGAKF PARLLVATGA RALLASPQAA
     PPQEAVRLRN GPQRREAETQ LRELMTKEVF PRDAAGLNPG ARAGGGSESR VDAQDGRQSD
     LQHAETKAPH GGSPPLALWL VGNALALLYG QLRAAELDQD ASAPRGVEKP VAAQRALLCL
     LCWGGSFVHD ALLRQSVLSS EEQHAASLSA SGRELRAQLR LLMAAGVLRA LFACADQDPS
     NRFPPLLRLF FPPSLCAESR PAEDTEADRV DGEAADLSES DEDLSDGAEA VMADVDAQGA
     EAPTSAPSLG MDRLILNALA MNTSLSAHLL PVIRLVLDEE CRGDVDEFLR QLGPAPLFDS
     PLGQVLRAAC TLLQYQLELM YDSELVDSAR MSSLSGFFPA PDPAASSASS ASLFCSSSSA
     PLLTVPDIQW LSLTLNKVAW KLLQACYAPP PAVSLSALRS PPATASAWAR LSPGALAILG
     GGTAGASRRV PAAGRGSALR PVLTTLVRQL FDRNSRLHFL PETSWILPET MSLLKSKALL
     HQQERLAQLD APFLAAAAAT EGLERVANSG VKHAEKILGA LLTELPHTLT FEDRVLVFYD
     KINADRLQYR DVAHQLPFDP SLHTIRRDYI VEDGLFALGY ADVHDLKGFF RIQFITDEGV
     PEEGIDGGGL FKEFLVLLSR KVFDPNYGLF KSSSDNSLYP NPSARLVHQN PSMLYTALGK
     VVGKALYEKI LIEPQLNRVF LNLLLGRPNQ VDDVQALDPV VHRNLLFLKH YSDNVQNLAL
     TFSVTLGDFG SNEEEDLIPN GRNISVTNDS KLRYIQAVAH YKCTKQIAKQ TQAFLHGLAQ
     VIPLKWLQMF SPAELQLLIS GSPRGFDVAD LREYAQFTGG FEASSPTIRW LWEILEDMTS
     EERSKFLMFV TSCSRPPLLG FRNLHPSFTV HRVPETHRLP TTSTCVNLLK LPPYESKKVL
     RERLLEAVEG TQGFGLS
//