ID   AKR2_SACU7              Reviewed;         730 AA.
AC   Q876L4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable palmitoyltransferase AKR2;
DE            EC=2.3.1.225;
DE   AltName: Full=Ankyrin repeat-containing protein AKR2;
GN   Name=AKR2;
OS   Saccharomyces uvarum (strain ATCC 76518 / CBS 7001 / CLIB 283 / NBRC 10550
OS   / MCYC 623 / NCYC 2669 / NRRL Y-11845) (Yeast) (Saccharomyces bayanus var.
OS   uvarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=659244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=623-6C / CBS 9787 / CLIB 533;
RX   PubMed=12594514; DOI=10.1038/nature01419;
RA   Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT   "Yeast genome duplication was followed by asynchronous differentiation of
RT   duplicated genes.";
RL   Nature 421:848-852(2003).
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;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR   EMBL; AY144797; AAO32361.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q876L4; -.
DR   SMR; Q876L4; -.
DR   PRIDE; Q876L4; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF01529; DHHC; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ANK repeat; Lipoprotein; Membrane; Palmitate; Repeat;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..730
FT                   /note="Probable palmitoyltransferase AKR2"
FT                   /id="PRO_0000212935"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          32..62
FT                   /note="ANK 1"
FT   REPEAT          66..95
FT                   /note="ANK 2"
FT   REPEAT          100..129
FT                   /note="ANK 3"
FT   REPEAT          133..166
FT                   /note="ANK 4"
FT   REPEAT          172..201
FT                   /note="ANK 5"
FT   REPEAT          205..234
FT                   /note="ANK 6"
FT   DOMAIN          429..479
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        459
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   730 AA;  83533 MW;  F7190729858C85A5 CRC64;
     MSEVSRDENM RGTSDGIGSQ AQFLESELDT EFVVETFIEA IKDDDLKVVK EVVESGAIDI
     NKDCIDELPG LHWACIKNRF SIAKFLIRRG ANVNQTAGPE RATALHWAAR YGHVYIVDLL
     LKHGANPTLI DGQGLNILHF SVYSSNIMLV VYVLYFVVSN NNNVDIDSRD YNNRTPLLWA
     AYQGDFLTVE LLLKFGATVA LTDNRGFNAL HCALVGGDQR AICDLILSGA NFYERNNQKQ
     DCFDLAKGMG TKALFEQALQ HHGYDKLGNQ KDKIFKKNSH SQLMIFLSPF ALMIYTYLIS
     LILSPPLAIA LSLLVIVVTV NSLKKFVLPS LTRKNIYKVS LVRTPFFSGL FMSTFSFLLF
     IWVKKLYPYS VFDYTAKDAQ LLITSLFTFV LFLKLVRSDP GCLKMDDSTT PVRETINQLI
     QIGKYDRNNF CVETLERKPL RSKYSLFSGA LVARFNHYCP WVYNDIGLKN HKLFMFFAFS
     VQYEMFLFMW LCLEYFKKTN HIYEQVEEYA KCTFLKNETL CKGSNYDPST FFLFIWISMN
     FVWLGGMLIV QCFQIFKGIT SPELYALIKE ERKAEALNLI PFENPIFSIP NGKNRDTVPE
     DPNATTVTHT ISIDSLEPRN RRHAILDACF SMVGLNQWVV TFKEMLGISN LLRGNSQPRH
     NHSLLRNFLV ANHWKTNLTD FWLNSDVTAP LWQRFFYSSD TSKAMLGGVE VDYYQLYELP
     AREGEPISSN