AKR1_ASPFU
ID AKR1_ASPFU Reviewed; 738 AA.
AC Q4X251;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Palmitoyltransferase akr1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein akr1;
GN Name=akr1; Synonyms=sidR; ORFNames=AFUA_2G07670;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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 -!- SEQUENCE CAUTION:
CC Sequence=EAL93064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000001; EAL93064.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_755102.1; XM_750009.1.
DR AlphaFoldDB; Q4X251; -.
DR SMR; Q4X251; -.
DR STRING; 746128.CADAFUBP00002314; -.
DR GeneID; 3513639; -.
DR KEGG; afm:AFUA_2G07670; -.
DR eggNOG; KOG0509; Eukaryota.
DR InParanoid; Q4X251; -.
DR OrthoDB; 445686at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
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; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13606; Ank_3; 1.
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; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..738
FT /note="Palmitoyltransferase akr1"
FT /id="PRO_0000212917"
FT TOPO_DOM 1..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..548
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 96..125
FT /note="ANK 1"
FT REPEAT 130..159
FT /note="ANK 2"
FT REPEAT 163..192
FT /note="ANK 3"
FT REPEAT 196..225
FT /note="ANK 4"
FT REPEAT 229..258
FT /note="ANK 5"
FT DOMAIN 455..505
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 485
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 738 AA; 82405 MW; 577E4236E35619A8 CRC64;
MSSGTPSTEP ESSGRSAGMS TSPTSIPAGK GTTTPPKVTQ QDVSVELKNM RPDRSPPKGS
IPLGEDIMQI ARIGEIGPMQ RLFDEKKFTA NYQDEEGITP LHWAAINNQY AMCKFLLDNG
ADVNAKGGDS VATPAMWAAQ RCHYYIVHLL LQHGADPLLT DVQGYNILHL ATIDGNAFLL
VLLLHQEIPV DVIDQQGHTG LMWAAYKGYP ACVDLFLRWG ANVNAVDDGG LTPLHWALVK
GSLPCVQKLI EYGADRFAKT RDGKSPATVA GEMNTTRVWY RALDECGYDV DGNTKVLPMG
LTSWLRNKSV MSKFFFLWPF LMVYAAVYIL SHMVIYAAIP IMLVATFGLQ WVAQKAASQA
PSEYRVLQKT PYLSGVFAGS LFWVGVTYIF SVLPATYSTS PILNILFAVF YCLTTYFYIY
SMTEDPGFVP KTGSRNQQKV VINELFEQWK FDEENFCVFC MVRKPLRSKH CKRCSRCVAK
HDHHCPWIDN CVGANNLRHF VLYIICLEIG IILFLQLTYR YINILPAPVE HACNIINEEL
CGFVLRDPFT LVLDLWIAIQ LVWVTMLCAV QLVQISRNQT TYENMRGHSI DRSYPSSRAF
ASAITAGTTS LEAAGLSATG QGPNPALARG HSHRGRRHGC LQQWSSLLGI DTFFATARDG
LRDGPRADRP KNPFSRGIIT NCRDFWCDPA PYFGKREPGT AMLGGEIVNY NQMYEVPMRM
YSDGRYQSVA HDDPEQHV
