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AKR1_CRYNB
ID   AKR1_CRYNB              Reviewed;         776 AA.
AC   P0CS67; Q55ZT8; Q5KP49;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Palmitoyltransferase AKR1;
DE            EC=2.3.1.225;
DE   AltName: Full=Ankyrin repeat-containing protein AKR1;
GN   Name=AKR1; OrderedLocusNames=CNBA4020;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Palmitoyltransferase specific for casein kinase 1.
CC       {ECO:0000250}.
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: Early endosome membrane; Multi-pass membrane
CC       protein. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL23286.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAEY01000002; EAL23286.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_777933.1; XM_772840.1.
DR   AlphaFoldDB; P0CS67; -.
DR   SMR; P0CS67; -.
DR   EnsemblFungi; AAW40964; AAW40964; CNA04190.
DR   EnsemblFungi; EAL23286; EAL23286; CNBA4020.
DR   GeneID; 4933661; -.
DR   KEGG; cnb:CNBA4020; -.
DR   HOGENOM; CLU_012510_1_0_1; -.
DR   Proteomes; UP000001435; Chromosome 1.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; -; 2.
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; 5.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW   Membrane; Palmitate; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..776
FT                   /note="Palmitoyltransferase AKR1"
FT                   /id="PRO_0000410346"
FT   TOPO_DOM        1..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..336
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..402
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..498
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        499..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        520..553
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        575..776
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          68..97
FT                   /note="ANK 1"
FT   REPEAT          103..132
FT                   /note="ANK 2"
FT   REPEAT          137..166
FT                   /note="ANK 3"
FT   REPEAT          170..199
FT                   /note="ANK 4"
FT   REPEAT          203..232
FT                   /note="ANK 5"
FT   REPEAT          236..265
FT                   /note="ANK 6"
FT   DOMAIN          454..504
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        484
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   776 AA;  84643 MW;  4F82A233DC8F2CBE CRC64;
     MDQEMTTVAS PDIRVKATSP DSNRAVLEQS IVLSDSGRLD EGSSIRGGEL ERDSQEVGRE
     TVREPLMCHD LDIHALAQRG DTAAIAAMLQ ENPSLNLSAR DAQDVTPLHW AAINAHMGTC
     RLLIDSGADI DAIGGELKAT PLQWAARNGH LYVVHLLISR GADPNIHDSQ GFNTLHLITH
     SSAVMPLLYM LHQPVAIDEK DTDGHTALMW AAYQGDALSV DLLIRHGASV NSTDNAGMTP
     LHWAAVKGNK VSIMHLVEAG ASLDAKEEAG KTPRDMAEEL RGLVPFQKGL EEAGWSIDGV
     KMEGKLGPRN TILAIFLLPI AVLWLIFSTF KWLPVYVGVP FAIAEFMGMQ YTVVLVLLGH
     IKAQDKVSTS NYFASIITAS LIWVGYCWIS RFAVNTPGYA FSNLGFIIMF VGCCWTFWTA
     IVTDPGFVPK GQQDAEIKEV LEDLVDAGRL NGTNFCIVCM ARKPLRSKHC RTCNRCVARF
     DHHCPWIWNC VGAKNHRSFL LFVLFLIGGI ILFIRLTIAY IQQNAPEYIP TPNPGLTTCD
     ISTTLCQAGD FDPFLLCMAL WSTLQLTWTS VLAISHLWQV SRQMTTFEVS NLGRYGFMGG
     RGGQSLRDQS GAMLKQAAAV GAGIGMSGAG EEAAGPPGAE AGPEGNALLP PPGGHVHGPQ
     CRHGDHARGH SHGVLHICGA LWKTLTGPLM TILGLDRFTK GKALGGMKRA GRDQNPFDMG
     MVKNCIDFWL PDNDVDYMTV YEIPPGGWRA YRRKLAMDKR VPGGKGRYEV VSEQEV
 
 
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