ID A0A1X7RV39_ZYMTR Unreviewed; 991 AA.
AC A0A1X7RV39;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Palmitoyltransferase AKR1 {ECO:0000256|ARBA:ARBA00016875};
DE EC=2.3.1.225 {ECO:0000256|ARBA:ARBA00012210};
DE AltName: Full=Ankyrin repeat-containing protein AKR1 {ECO:0000256|ARBA:ARBA00030960, ECO:0000256|ARBA:ARBA00031920};
DE AltName: Full=Palmitoyltransferase akr1 {ECO:0000256|ARBA:ARBA00017919};
DE AltName: Full=Probable endonuclease LCL3 {ECO:0000256|ARBA:ARBA00013404, ECO:0000256|ARBA:ARBA00014651};
GN ORFNames=ZT3D7_G6402 {ECO:0000313|EMBL:SMQ51249.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ51249.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ51249.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase specific for casein kinase 1.
CC {ECO:0000256|ARBA:ARBA00002100}.
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; Evidence={ECO:0000256|ARBA:ARBA00001870};
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004520}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000256|ARBA:ARBA00010104}.
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DR EMBL; LT853696; SMQ51249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RV39; -.
DR STRING; 1276538.A0A1X7RV39; -.
DR Proteomes; UP000215127; Chromosome 5.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016409; F:palmitoyltransferase activity; IEA:InterPro.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
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 Pfam; PF00565; SNase; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 79..111
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 113..145
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 180..212
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 213..245
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 800..959
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 110404 MW; FB9F6E807202DC03 CRC64;
MASREASRPS SPGRRDSGSA PSSPTKDGLD KVELSDLDAS PPQLPIESDL MQLARLGELR
AIQKLFDSGR YTARSTDEQG ITALHWAAIN GHHALCHFLV QSGADVNAKG GDAQATPVLW
ASKKFNLQVI SLLLTNGADP LIRDDQGYNL LHSATLDGNV YQLILLLYQS DIPVDVQDAQ
GHTSLMWAAY KGFPACIDVL LRFGADVHAT DDMGFTSLHW ALVKGNYLCI QKLIEAGSDR
FAKSKPTEGE TEGDTPSMTA SKMKSDRQWR KALLESGYDE HGCPQKFPIP MVHDRRLFFQ
RFFFLWPFAL GGLQLHMLAY LNVWVSVPGV LIVGYGLQFA VQKLLRWAPS DMNSMHKTPF
LAGVFAATLF WVAVRFIFKI FPNTLFSNFF LTVAFTTCMC LTTYFYTMTM TADPGFIPKG
ASRGQTKKTI DELVEHNAFN EAQFCTTCMI RKPLRSKHCR RCGRCVARED HHCPWVDNCI
AVNNHKHFIL YILSMVAGIA LLIRLFFAYL TILPAPTKPI CTFLNPELCA EFEKDPLTLV
TTAWASVQLT WTVMLVFVQF FQVARNLTTF ESMRNTDQVG PILSAITTGT MSMDDAQVTG
PAAGSSHKHA HRKKEGCLAR WSKLLGIDTF LTIAFQGYNG AKDSRSPSRT PRRKQNPFSR
GVVRNCQDFW CDGPVFGRKV GNEGLVGGER VDYGGLYDVP GGGARGWRGY EAVPALAEAG
RPFAMLWKKQ SSEEASKPNN ASTSPPPPSR PGKQPWTNTS VALTVVVSVT ASWAALRFYK
RFLRRIPNIS HLHPDALRTR SLYGYVTRVG DGDNFRFFHT PLGIFAGWGW LPSRRVQDLG
KKELQDQTLH VRIAGVDAPE CAHFGRPAQP YSAEALEWLK GTVEGRYVRV YPLRKDQYER
VVGKVVSRWV RKDLGTAMIK TGCATVYEAK FGSEFAGLEE VYRKEEEKAR AGGKGMWKAP
GLVGRILGGK GEVRESPREY KNRMKAEDMA K
//
