AKR1_GIBZE
ID AKR1_GIBZE Reviewed; 725 AA.
AC Q4I8B6; A0A098DNJ1; A0A0E0SAH8; V6RE25;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; ORFNames=FGRRES_06542_M, FGSG_06542;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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 -!- SEQUENCE CAUTION:
CC Sequence=ESU12646.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS231666; ESU12646.1; ALT_INIT; Genomic_DNA.
DR EMBL; HG970335; CEF83441.1; -; Genomic_DNA.
DR RefSeq; XP_011326153.1; XM_011327851.1.
DR AlphaFoldDB; Q4I8B6; -.
DR SMR; Q4I8B6; -.
DR STRING; 5518.FGSG_06542P0; -.
DR PRIDE; Q4I8B6; -.
DR EnsemblFungi; ESU12646; ESU12646; FGSG_06542.
DR GeneID; 23553671; -.
DR KEGG; fgr:FGSG_06542; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G22541; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_0_1; -.
DR InParanoid; Q4I8B6; -.
DR PHI-base; PHI:1675; -.
DR Proteomes; UP000070720; Chromosome 4.
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; -; 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; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..725
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212924"
FT TOPO_DOM 1..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..326
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..547
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..725
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 84..113
FT /note="ANK 1"
FT REPEAT 118..147
FT /note="ANK 2"
FT REPEAT 151..180
FT /note="ANK 3"
FT REPEAT 184..213
FT /note="ANK 4"
FT REPEAT 217..246
FT /note="ANK 5"
FT DOMAIN 451..501
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 481
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 725 AA; 80316 MW; 7218BD622651F67C CRC64;
MGTIAMASIN TTSTSGGSAA PIQMSGKANA ATPKLNSEVE MGSLPGDAQT QEDDIMQVAR
VGDVPAMEKL FESGEYDATY HDDEGITPLH WAAINNQYAM CKFLIEHGAE INRKGGESIA
TPLQWAAQRC HYYTVNLLLQ HGADPLVTDA QGYNTLHIST FNGNVLLLVL LLHQGIPVDV
IDTFGHTALM WAAYKGFPQC VDLFLRWGAS VHATDEQGFT ALHWALVKGS PGCILKLIEY
GADRFAKTQT GKTPSVTAKE LNTEVAWHRA LTECGFDEDG HPAVPPWPGA SYFLKDKRSF
VTRFLFFWPF VLVWAMLVAM SSAPVYIGVP LGIAAVYAIQ WVAQQVLEYA PSDMRHFHKT
PWLTGIFAAT LFWTGVNWLT TVLFATTLGA PEGKGHGILN FLFALFFGFT VYFYIASMRY
DPGFVPKMNG IAEQKAVIDE LLAQWKYDET NFCVTCMIQT PLRSKHCRRC QRCVAKHDHH
CPWVYNCVGI NNHRHFFFYL ISLTMGIVSY DFLLYYYFDT VSKNASETCN VLSPTLCKYI
NADSYTSILA IWITMQLLWV TMLLFTQFIQ VARAMTTYEN MFGIRDGTNI TALTSTGAPL
DPNHPSLSAT GPAAAHSHKH KGGMLKSLSR TLGVDPFIET ITGRGAVSGK NKRKKKNPYS
KGCITNCKDF WCDPAPIFGQ RENGSAVLGG ERVDYSAMYE SPSLMTITGR RDRGGYEAVG
TEDVV
