ESTE_HVAVE
ID ESTE_HVAVE Reviewed; 655 AA.
AC A4KX74;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 23-FEB-2022, entry version 44.
DE RecName: Full=Putative esterase;
DE EC=3.1.1.1;
GN ORFNames=ORF19;
OS Heliothis virescens ascovirus 3e (HvAV-3e).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Ascoviridae; Ascovirus.
OX NCBI_TaxID=260797;
OH NCBI_TaxID=7100; Noctuidae (owlet moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17374755; DOI=10.1099/vir.0.82651-0;
RA Asgari S., Davis J., Wood D., Wilson P., McGrath A.;
RT "Sequence and organization of the Heliothis virescens ascovirus genome.";
RL J. Gen. Virol. 88:1120-1132(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; EF133465; ABO37205.1; -; Genomic_DNA.
DR RefSeq; YP_001110871.1; NC_009233.1.
DR SMR; A4KX74; -.
DR GeneID; 5076189; -.
DR KEGG; vg:5076189; -.
DR Proteomes; UP000001324; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..655
FT /note="Putative esterase"
FT /id="PRO_0000330602"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 515
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 655 AA; 74351 MW; A7735800A5AEEBEF CRC64;
MCKSRLPTVL SLTLIYISIS IGFSVYFYVL MEAAYDQFSS MFESYTQTAV HLQSNSRTLK
SDLSDYMQLL NYSRKFDESG EESVLRRHNI TTPRVFYIDL NYTTALGAEN RNLNMINFYA
IPYRYVDLLD PFGNSIPVTG RTPATEYIDC SRDKKEKCID SIPPFDGVLD CLSLDIHMQP
WSRNNKSFNR PIIIWLGEVA GELWRLVAGG LIVIRANYRR GCYGFLCHHD QSLPYRNQGV
NDVLHAIDWT IENARHFAGD ISKITLAGHG ASASLVEYIR LNHGHHLPLD KYIVMSANNF
GSRDLYCSSN SNVMVTTARL LGMPPSPATE SGKERSVYES VRYLSFVEPK LVMSKLYGLK
AAFHPCPLSV NNRRASTFGI GFKTKNHTSS NCIRTANEQP VLFTNTLNEY HNFVYGSTVF
THARSETILR TIGDMLSRHF IESRLAYANS STEKLIQQVN GQYNVVDGEF VDYDAFIRLL
TDFAFIMPTV KMNEFTTECG GNSYHYVFDF GNSTHGDDLK MLTSSANDTS LTHFQRQLAD
GLGFILSKFV RRGYPVKKQD GWCPSTGLVA QIMEMNTKDE NVVVKKSTEG VLIPLLNQSY
VLHFHRVSVA KQKCYNRLGN VPFWNDLLKF HQSARRGWRD GDTGCARSKY LSEIV