ID A0A098VUD4_9MICR Unreviewed; 2812 AA.
AC A0A098VUD4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=DI09_156p10 {ECO:0000313|EMBL:KGG52587.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG52587.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG52587.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG52587.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG52587.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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};
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:KGG52587.1}.
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DR EMBL; JMKJ01000062; KGG52587.1; -; Genomic_DNA.
DR RefSeq; XP_013239023.1; XM_013383569.1.
DR GeneID; 25258527; -.
DR VEuPathDB; MicrosporidiaDB:DI09_156p10; -.
DR HOGENOM; CLU_227466_0_0_1; -.
DR OrthoDB; 2787957at2759; -.
DR Proteomes; UP000029725; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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:UP000029725};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 2443..2780
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 2766
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGG52587.1"
SQ SEQUENCE 2812 AA; 326186 MW; 48F758260141FEC1 CRC64;
MLCEIFKVAS PDPKHEYLWK VLIYNSGDGL EHHPEYHIGP RKQYSPVVIY EGPPFLINEA
WIEAALNFGN HEKVITNFYP RLLGAFDRSN ATYDVFIDPK RNGTCAISSY RAYCTFKLTE
SVCKKIFLVA SLSGLQHFVS EQSSDFVSQK YRIKYSLSLP SQPSHSIEDK NGAENFMYEK
LTSNRDILNE MAKFQFLRWN VDLVDTMFRY LVEIGNGVFE MKEHVFFRDL KLAYDQFQIA
RKKNIFDAVP THIADNRGIR AFFSGPDWSI FNLGPLDKLS ANETFYCELP NFEYQDGGYD
RQNFSEFSSS ILHFFDQRNR LSALLYGQRD SSDFISRFAD IPGHANVEIF KAYKEIYITY
LKDSLNSDEN KFKVINDRIF EKLSPSFSYS DEIDLLERIL PKSKKFISFL DGDIEITSKL
VSILFKDSKD LPNPDEMGQF FNVDMIKDQI GSASDYNYDP EHFKRSLYIL TVVSNPIRIE
SSNNTAIPKN FLLDGHYYNL LDLLYKILDI NYSPYVSGAT FRLYFGIPTY FISSLKVKTH
DYDITEEIAS LSSKEKRPLG LMGLDPKFSS GFSFLNYDQK DDAFILSEAG MKILYTFLLR
PSTYDNDHTK EALPPVIEYF LSRRDKILSE IFINGDDTEL FRLLANYQII LNRLMSIQKT
DLDIGDLEHV FVAQYQPIFA FLKLNTLIVG EKFSNLTNSH ALYLSVISNF ELIKSFFCKE
EIQYVLRIYY DNWRFSSSKS RCAAQTEKGI QNLVNGHFLI DGETRQLLRL PSQNHSLWTA
MGIDLNRKYK LEFTLYKRRA DGSIFSILKY NSMYFILHKN DAFLVKNGQV EAKYIPQDFK
LCHSHLDLKI AFNSKMVGSD HNIIAFKRCF ESWWMWLWMW LWSWLWSEEV FLLFDKDGFP
YGKIYGTNTL VLENSSKFVG NLSSPLPCSF HINSFCSFSS QSFFDDFSNR EPIFNFVFYS
YIFMLKSQAQ SFYFFDSYNG PAKDFYVVKE GGEQYFAVIK GEKFKIHPPA EIKENFLVSS
NLPLLFVSIG KSFQIIIPVP LSKPGDSYNF TFVSATCKDD HFNIEGHDRE INLAIAYWLV
FLKYYDRAME YVSLYSSVSL QLTELELVIL QNILEIKYRD VEYLVIEAWA NHFLDEHDIF
FKGFLDETNR VEKITKIANL ISVIPFKYKR VLFSFLPNIN EHKYLWAYSN KLKIGSSIGK
PAEFRLDIPS LKKDIQDAEY ELSQNSFLKI ELTDWNILKN IHFPSCLSFL YKLAGSSNDL
TDFVDKLNSH YVDFTRFYLE MENDKDGYKI ISLFYVIFMV FNKLPDKENL VTFFAKFKKN
TFPYELLDIY DRSVKFKSSI PYEGSFNITE ILPSSPADYE NLLNITMQRK ALSSDLFKAN
VSFTFFSDAA SLEEKLKSIV STDEFLYGFP LGALKDPRLL AQILLCGSVE ELGAFFTVSA
EKVPKLLDLL WSHFITVFYC ESPLLKKNTF CKAWIEKKHS FPQQAEEIPG QKLLVTMQDK
VFILIEFFAK YPLREQQRTI MSTILHKIVD EESYAVEQEI DGASTMRFGP AIAIMARSVL
RKLPIFIFSN SILDQNILQL RQWLFDFFGK SVFEFKTERS DYGYSEPYLR YLYYQLTMAH
DRGDVFVSSM NSIQCLLNAK KELFSQNTDE SKETLAWVLR ILHFIEHYSM VVFDEVDASA
LYSFDTNEPA EKDWNLIDVL IECFLSLKDK KIFRSQTGEE ITIFEIKEPL TPSTTESFKN
TLNKALEKML RKTSKEIRAL IIDQLFVSCW EKVRNVGYGA SMKSSVPYPI PYSMANTPRE
GSSFGNQLFM IAISLKFYLE NEMKDLSEPP LFFTKANIYS TLKILDYDPV KLMQRTPKLS
HLQLFNHLRD KIYETNQTFD KFLRNVVIKN IKTSRDLLAS SAQEALLYFS QFIEFRKHPS
CNLEMLKFIS NLEIYDKRSF VRGSQSLKSV AFPAQNCYTK DDHSEIDYYA MLTKKSLGIC
MPKDHEFKAF MDFIFKLNTT ALLDVGAVLK DYCNSKVAKK ILDSKKYRCV VYYDEKQNVI
VYQMDTGRVG RDLPVEGQFS FLETRYGLKN KDIFLYLDQA HCFETNVDVN NPSAICVVTF
STLVSAKYFH QALLTARELL NGISHMDPLS HAEDPRHQIK IFVSSILRYD KAMHSTLSEE
ERETLSSKAD LFPKDMPADK KAALQTIFTS AHLNQLTRDR RERDLLPWQV FFAKLLKSFW
SPAYSAGSKI PNWNTILNLN DTKSIDQLKK ILFSQTGISK SKILKLFEAN EILKKFSPNL
DISSIPEVEY SCALDVEAVL KDSQEIHANV KDANVAPAKP LSFSRSAPEI PDLSLGFINY
LENIDSVSIK SDVTSLRHFY NVHFFIVQNL ICIYNRLVNL VPEWVFQYLL LMSFGADTNP
IIRNIGIMAG LFHKKFSIKV RRDDIFRSSF TAFKRILSIP KEHSALLHIH SFEVEFLNEE
GVDAGGLSRE WATLMAAQLQ VSELSIFNSY KEGFYFRRDG KNKEYAKFCG AFLGLAISKE
LTLDCRFSDL FYRILTSDPK NIPLLFKDME LIDTDLHRGF SNSDSNLLND LENFYKDGDD
KKKLDFFKAC KRYLIVSPDE KIGAHLPRDK DGETFTSIVL TDDDLNSLRD ELTHEIYYSA
LKDTIERFLD GVHIFIPPEE LQLFSIEGLR KKVEGEFSEI NDKAFEKWKA ITVWKYLTNG
KTGIEEETWK NGLKIQKDWF WEIIQKFSEK EKRDLLQFWT GSRNIPKTLE VNHGGTVNYF
PSSSTCLLSL NLPYYKDEKV AVDGIETIKG AKEIMKEKIL EALKLRSGFQ FV
//