AKR1_ASPOR
ID AKR1_ASPOR Reviewed; 737 AA.
AC Q7Z8U2; Q2TZB1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 114.
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=AO090011000927;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ishida H., Hata Y., Kawato A., Abe Y., Sano M., Machida M.;
RT "Molecular characterization of the gene (sid2) encoding non-ribosomal
RT peptide synthetase and the clustered genes involved in the ferrichrome
RT biosynthesis of Aspergillus oryzae.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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}.
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DR EMBL; AB087621; BAC78655.1; -; Genomic_DNA.
DR EMBL; AP007171; BAE65354.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7Z8U2; -.
DR SMR; Q7Z8U2; -.
DR STRING; 510516.Q7Z8U2; -.
DR EnsemblFungi; BAE65354; BAE65354; AO090011000927.
DR VEuPathDB; FungiDB:AO090011000927; -.
DR HOGENOM; CLU_012510_1_0_1; -.
DR OMA; PWMAGIF; -.
DR Proteomes; UP000006564; Chromosome 7.
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; 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..737
FT /note="Palmitoyltransferase akr1"
FT /id="PRO_0000212918"
FT TOPO_DOM 1..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..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..737
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 228..258
FT /note="ANK 5"
FT DOMAIN 455..505
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
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"
FT CONFLICT 232..234
FT /note="TPL -> LP (in Ref. 1; BAC78655)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="K -> N (in Ref. 1; BAC78655)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> R (in Ref. 1; BAC78655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 81525 MW; CB5EF23024CD2E39 CRC64;
MSSGNSSTGT HTNGNFATLG SSPPSAVGGK GRAIPPKVTH EDASVELKTM NPERGAARGS
IPLGEDIMQI ARIGEVPAMQ RLFDEKKFSA NHKDEEGITP LHWAAINNQY AMCKFLLDSG
ADVNAKGGES VATPAMWAAQ RCHYYIVHLL LQRGADPLLT DVQGYNILHL ATIDGNAFLL
VLLLHQEIPV DVVDQQGHTG LMWAAYKGYP ALVDLFLRWG AHANAVDEGG LTPLHWALVK
GSLPCVLKLI EYGADKFAKT RDGKTPAVVA GEMNTTRVWY RALDEYGYDL DGNAKVSSSG
LASWVRNKSL MSKFFFLWPF AIVFAAVWIL SNMVVYAAIP MMLVTVFGLQ WVAQKAASQG
PSEYRILQKT PYLSGVFAGS LFWVGFRYVF YVLPVTYSTS PILNGLFAIF FSLTTYFYIY
SMVEDPGFVP KLGSRNQQRA VITELFEQWK FDEENFCVSC MVRRPLRSKH CKRCARCVAK
HDHHCPWIDN CVGANNLRHF VLYITCLEVG IVLFVQLTFN YINSLPAPAQ PQCNIINETL
CDFVLRDTFT LVLDLWVCIQ LVWITMLVAV QMIQISRNQT TYENMRGHSV DRSYPSSRAF
ASAVAAGTTS LNAAGLTSSG QGPNPALAQG APRHRKHGCL QQWSSLLGID TFFATARDGL
RDGPRAVRPK NPFSRGVVTN CRDFWCDPAP YFGKREPGAA MLGGEVINYN RMYETPSRMH
SGGGYQSLSV EDPEQGV
