ID V6TUF7_GIAIN Unreviewed; 556 AA.
AC V6TUF7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=GSB_153131 {ECO:0000313|EMBL:ESU42623.1};
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741 {ECO:0000313|EMBL:ESU42623.1, ECO:0000313|Proteomes:UP000018040};
RN [1] {ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GS {ECO:0000313|Proteomes:UP000018040};
RA Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA Nash T.;
RT "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT Pig).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESU42623.1, ECO:0000313|Proteomes:UP000018040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS {ECO:0000313|EMBL:ESU42623.1,
RC ECO:0000313|Proteomes:UP000018040};
RX PubMed=24307482; DOI=10.1093/gbe/evt197;
RA Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA Nash T.E.;
RT "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT Pig).";
RL Genome Biol. Evol. 5:2498-2511(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000256|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000256|RuleBase:RU079119}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000256|RuleBase:RU079119}.
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:ESU42623.1}.
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DR EMBL; AHHH01000076; ESU42623.1; -; Genomic_DNA.
DR AlphaFoldDB; V6TUF7; -.
DR EnsemblProtists; ESU42623; ESU42623; GSB_153131.
DR VEuPathDB; GiardiaDB:DHA2_152895; -.
DR VEuPathDB; GiardiaDB:GL50581_2859; -.
DR VEuPathDB; GiardiaDB:GL50803_008619; -.
DR VEuPathDB; GiardiaDB:QR46_1937; -.
DR Proteomes; UP000018040; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR22883:SF286; PALMITOYLTRANSFERASE ZDHHC4; 1.
DR PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU079119};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 21..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 62..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 176..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 207..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 129..257
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 346..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..378
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 62564 MW; 790D7C2BD85ECE8F CRC64;
MLIKLSKDIK IRWYGANRVM MGGRIVIGSQ PCFLIGTICL VMAALAIFWA GFYLSKSNPR
HLAWHIIAHI LLDGSLVASL VMLLITGLTD PGIIPSAQFD RELIPILSPA TKLSDNSRDR
IISHNGYTMK LKYCETCFYL RPLRTTHCRT CNCCVYRFDH HCFWLGTDVG YRNHGYFYIM
LLMVTIYISL LLLCSLVVVG FSIYDCIIYP FSVGFAISFI SEAIILASGI YMLYSLANLI
SYHVEILTGG LLTKEDLASN LIEDHPYHHK SFKRNFCACF EGMGAPSVLY QVINSYKLVA
QNKEELDALV KAGLNPRVFP DDVAQIRTAG QAFEYLISMS KSQIVNPPMD TKQELAQKED
AEEEEEEEEE EEEEDLKNER DEERGSKFID ATMVNVQRIE EIKRKSIRNI VGSVDTLSNP
GSADMRKGSI DKRLSKRGST VIYEQSDDET PSRRKVIDLD NLQTSNRASE RMSTKLPVLL
SVRNSLNKSS HSTNNRSSTR GSVVMSQQLV ERITKLQSQQ SKDPRAINDA VHQGSTSMVL
PPLPPPEASY KPGRSS
//
