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Database: UniProt
Entry: A0A0L0C605_LUCCU
LinkDB: A0A0L0C605_LUCCU
Original site: A0A0L0C605_LUCCU 
ID   A0A0L0C605_LUCCU        Unreviewed;      1498 AA.
AC   A0A0L0C605;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
DE   Flags: Fragment;
GN   ORFNames=FF38_11339 {ECO:0000313|EMBL:KNC27715.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC27715.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC27715.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC27715.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC27715.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC         phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000815};
CC   -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00008389}.
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:KNC27715.1}.
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DR   EMBL; JRES01000857; KNC27715.1; -; Genomic_DNA.
DR   STRING; 7375.A0A0L0C605; -.
DR   EnsemblMetazoa; KNC27715; KNC27715; FF38_11339.
DR   OMA; MRVQGHL; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1.
DR   InterPro; IPR044611; E3A/B/C-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR   NCBIfam; TIGR01544; HAD-SF-IE; 1.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF05822; UMPH-1; 1.
DR   SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   3: Inferred from homology;
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1161..1498
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          677..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1466
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KNC27715.1"
SQ   SEQUENCE   1498 AA;  171805 MW;  F4B1AFD90246E019 CRC64;
     AAAPPIFTRI LDRIMMGSST EMNQQEDNTM DEISIRLQDI KQLCDDHCKI KDPARVERIL
     NEFVRGGTER LQLVSDFDYT ITKQRTADGK PVLSSFGILN ACKSLPANFI EESDKLYHKY
     RPIEIDPHIP TKDKIKHMID WWTKTGELLV GFPLGQSEID GIAGKYKDAL RDRTNVLFET
     LNRLDIPVLV FSAGLGNSVI SVLQQANVMY SNVKVVSNFL QYKDGLLNGF QQPMIHTFNK
     NETALDGSEY YDLVHSRDHI IVMGDSIGDA DMANGVPSSS HIIKIGFLFD HPEQNLERYM
     NAFDIVLIDD QTMDVPLALL SAIENFQQRL QSNSTSKNEA QIKKGQNHYK KIMFGFDGEY
     RRKPSQSFGG ASTSSDRETI IRKAAEERLK RNQMRRENNG AIVLQSYLRS FIHRQRRKRY
     ERETFDEFLR THRDKLTQDE NLAFLLKRII FFYNTKETKD GERLIDICQH VLKNPARLVQ
     NSTTDAVWLH RLKKLLDLCI IQLTSVQQTS QAIPLRMLET FTAETSIERY VENEQLIQTY
     LDRIFRYLVD KDYYKRLREL LEQKCPPLDG ETLHPPNQFS EAIYQLMLRP LLLANKAASG
     FSYGNIICQS FTKHILALPY TDCIRYFLLP CFAECSEFPF EYLLKTLQQC TRTQLPEKMQ
     IDSSPVVTFT GASAAESLNT TSNSSSPSSN KGMEDKSQEP TKIFSTFLLH SLLMLDRKQL
     KSLHAKSLLG DYIKVIAEVS PKILQLPKSS LKHTGHHQRY HPHASEDTSS DDDSEDEEEE
     DQYQNKRNLQ SMDTVDVMTM SIPLSEIEKD SLLECIQLLN EGERVHSILD YIEEYLKDED
     VLYGLCEICH NLMIYNKMAM FEYKLLYTLA FMPNFIRAVW FTLIAQSKQQ GFNAPLTLIS
     KGVVPKQAGA ESFVPLLATF CMLFGRLLPT LHDVEFCDEK LLIEKPLQPT LHVRLMPFSL
     AEIVQLSKTL KEVSLGLVEL AFPETRSNLN QHYRFVLGRS DSDDKKIKQQ KLIWSNLLKV
     VVFVLNQIHT RDLRLGFCPE LHWTVSRLDL PLDRPADLPL TRGSRTRGIR PFQPIRDFTR
     EDFENGPPMS TKQIRSITIL REIPFVVAFS KRVGILQGLV AADKMRVQGH LQAFLQGPSI
     TLTVRRTHLY EDAYDKLRPE NEPDLRLKFR VQFVSSLGLD EAGIDGGGVF REFLSELIKT
     AFDPNRGFFM VTTDNKLYPN PNVGDLVPDF EKHYYFIGRI LGKAIYENLL VELPLAEFFL
     TKLAGKYADV DIHQLASLDP ELYKNLLYLK DYEGDVSELN LDFTVASSSF GQTQVIELKP
     QGQSIPVTNS NRIEYLQLMA DYKLNVQIRQ HCIAFRKGLS NVLPVEWLYM FSNKELQILI
     SGAEIPIDLE DLKKHCKYGG EYSPEHPSIV AFWSALESFD DLQKRQLLKF VTSCSRPPLL
     GFKDLDPPFF IQNAGDMERL PTASTCTNLL KLPPFKTVEQ MREKLLYAIQ SGVGFELS
//
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