ID AKR1_USTMA Reviewed; 844 AA.
AC Q4P6L3; A0A0D1C1N5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; ORFNames=UMAG_04250;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CM003151; KIS67752.1; -; Genomic_DNA.
DR RefSeq; XP_011390722.1; XM_011392420.1.
DR AlphaFoldDB; Q4P6L3; -.
DR SMR; Q4P6L3; -.
DR STRING; 237631.Q4P6L3; -.
DR EnsemblFungi; KIS67752; KIS67752; UMAG_04250.
DR GeneID; 23564493; -.
DR KEGG; uma:UMAG_04250; -.
DR VEuPathDB; FungiDB:UMAG_04250; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_0_0_1; -.
DR InParanoid; Q4P6L3; -.
DR OMA; DVPDCNG; -.
DR OrthoDB; 33889at2759; -.
DR Proteomes; UP000000561; Chromosome 12.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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:SF17; PALMITOYLTRANSFERASE HIP14; 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; 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; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..844
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212932"
FT TOPO_DOM 1..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..559
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..844
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 65..96
FT /note="ANK 1"
FT REPEAT 101..130
FT /note="ANK 2"
FT REPEAT 135..164
FT /note="ANK 3"
FT REPEAT 168..198
FT /note="ANK 4"
FT REPEAT 206..235
FT /note="ANK 5"
FT REPEAT 239..268
FT /note="ANK 6"
FT DOMAIN 459..509
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 18..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 844 AA; 90932 MW; F39CF0EB64690F1B CRC64;
MAAPGTPLSS SATQAISVST VDAPSDPLLS SQSAQLDGHS SWDTHMGGSN GIGSRAPSRA
NTPGQDQMPL TIHSAAQRGD LPAIMRLVDS GRATVHDRDD DNITPLHWAA INAQLATCRY
LLDHGAQVDA LGGDLIASPL QWAARNGHVY VLELLCSRGA DPTITDSQGF NALHLTVHSS
AVMPLVFMLQ QPSLDSPEGL DSTDSQGHTA LMWAAYQGDA ISVDILLKHG ADVHKRDGAG
LTAMHWAVVK GNRLCIRLLA DAKADLLAKE DSGKTPRDMA IELKSIGAYR KALADIGLEE
DGRRKQRTFG ASTDRTARLA TMVVPFVALG FIFATFAALP WYTAAPFAAA ELFGMHHIVT
RVILDPHEHD FLQRSNYFLA IVAGSIAWVG WEWVHKLASA TPGYASNNLF FALSLIVCSW
NLFRAASISP GYAPLVPSAL HRREIVTQLA QQGRLNGQTY CVSCMARKPM RSKHCKLCKR
CVARHDHHCP WVANCIGVGN HRQFLLFVGA LVVGVLQFLY LTVVYYSINA PPYDPLPDSS
YETCHLPFAF LCTATTFDAF LLGVALWAAL QLTWTVILLV AQAWQITRQM TTLEVSNLGR
FGFMGGKGGQ SYAGQTNFIA QHSGRGQPSG SLSAATDRLQ GIHKQFGENE NAEIDVNLGA
DESADATSTH AHAHGSHSKL NLLRRVFASS SSWLLSIVGL DLYTRGKAGE GLKRASAAAN
PFDHGLLSNC KDFWSRGEDL NLDYTTLYDL PAEVSPGHCQ VVPFLVDTVT AGGRGGAWRN
RSPASGYSLL RSGADDDDDD SDNATMPVDA AGRRKWSMWS NLKKSAKPPG SATAILPTSN
ATHA
//
