ID A0A1R4AAN9_BABMR Unreviewed; 635 AA.
AC A0A1R4AAN9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=BMR1_02g02971 {ECO:0000313|EMBL:SJK86061.1};
OS Babesia microti (strain RI).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=1133968 {ECO:0000313|EMBL:SJK86061.1, ECO:0000313|Proteomes:UP000002899};
RN [1] {ECO:0000313|EMBL:SJK86061.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:SJK86061.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=22833609; DOI=10.1093/nar/gks700;
RA Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
RA Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
RA Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
RA Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
RA Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
RA Ben Mamoun C.;
RT "Sequencing of the smallest Apicomplexan genome from the human pathogen
RT Babesia microti.";
RL Nucleic Acids Res. 40:9102-9114(2012).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO082872; SJK86061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4AAN9; -.
DR VEuPathDB; PiroplasmaDB:BMR1_02g02971; -.
DR OrthoDB; 230345at2759; -.
DR Proteomes; UP000002899; Chromosome II.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24161:SF85; LD20463P-RELATED; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119,
KW ECO:0000313|EMBL:SJK86061.1};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Membrane {ECO:0000256|RuleBase:RU079119};
KW Reference proteome {ECO:0000313|Proteomes:UP000002899};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:SJK86061.1};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 306..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 334..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 518..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 552..575
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 83..115
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 192..224
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 225..257
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 471..595
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 635 AA; 72872 MW; 599A9591477E9121 CRC64;
MTTQAIKMPD FGFDRLNTKL EESLITPVTH VTIAESSRST PIQTLSPQQL ERTLFNAATN
RNLCQFYSTI QPLLLAGNIS LCDDIKALHW ASFCGNAEIV KKLLDIGCDV NKVDSINGET
PIFFAIKGGS FATIHYLINR FGTPIIVHKN KRGMTPFLVA AAEANQDDIS TALRILELFY
LYGVSLEEQD ENGMTCLLHA ARRGSLHVVQ WLLARGASLA HRDFLGNAAI HYACFSGNLE
TVRFICQKGA PSFMDSKSIA KTSEEQTVWG ICKLKRNLLL YLLMKIWKLQ GVITGHISSL
RSPYPFYYWG ITIINMLLFM NMYHTLEINS DCNIWFLLWV CCQIFWASTF FSDPGFAKAQ
VVPTQKQITS SFYESDCYQP SVHMFHPQSY SAHLEKLERR QKFINLEIYK VKMDGGTNGY
HQYHDSSGVC LEEGKMLCIE MHSIYDKVAL ERRANSHPKY VEAVMDINGD YKSVCVTCSM
IKPRRSHHCG ECGHCIIRQD HHCAWVDNCI ARDNQRSFFL FVFTLTLLFL QNYKVIYLYM
VSRCYLLEGQ MIWAFFTCIF GACFNTFWLL FVLYLTIRTA RSSLTNVTFY EMLKKPEYIR
DKYGECNTVC WDFKGLNPIK AFQNLVSFCS RDDSF
//
