(data stored in ACNUC7421 zone)

HOGENOM: DESAT_1_PE447

ID   DESAT_1_PE447                        STANDARD;      PRT;   577 AA.
AC   DESAT_1_PE447; D6Z007;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Apolipoprotein N-acyltransferase; (DESAT_1.PE447).
GN   OrderedLocusNames=DaAHT2_0458;
OS   DESULFURIVIBRIO ALKALIPHILUS AHT2.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESAT_1.PE447.
CC       Desulfurivibrio alkaliphilus AHT2 chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D6Z007_DESAT
CC   -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins
CC       (By similarity).
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl
CC       transfer).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- GENE_FAMILY: HOG000264279 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D6Z007; -.
DR   EMBL; CP001940; ADH85164.1; -; Genomic_DNA.
DR   RefSeq; YP_003689783.1; NC_014216.1.
DR   ProteinModelPortal; D6Z007; -.
DR   GeneID; 9256398; -.
DR   GenomeReviews; CP001940_GR; DaAHT2_0458.
DR   KEGG; dak:DaAHT2_0458; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:HAMAP.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_01148; Lnt; 1; -.
DR   InterPro; IPR004563; Apolipo_AcylTrfase.
DR   InterPro; IPR003010; Ntlse/CNhydtse.
DR   Gene3D; G3DSA:3.60.110.10; Ntlse/CNhydtse; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; Ntlse/CNhydtse; 1.
DR   TIGRFAMs; TIGR00546; Lnt; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   HOGENOMDNA; DESAT_1.PE447; -.
KW   apolipoprotein N-acyltransferase;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Lipoprotein; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   577 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGMGGMGKIS LAALSGLLLF FSSPGSGGHA LLAWMALAPL LLAIQQLDWR RAAGLGLLAG
     VVYHLPLLHW ITIVLGDYGG VHPLVAALAL GLLVIYMSLY PAVFAALLVT LTGWGGNDNR
     HRGLVLWAPA VIWVGLDVLR ARLFTGFPWQ DLGYSQYQLP LLTQVADLGG HHAITFLIVL
     SSTLLALLVI VQQHRIFGRS AKLTYRGYAA LDCLPEPAAL LNDYGTSDRQ VGTPGERFPY
     RRTVALPGRW SLALAVLLLI SSVAYGSLRL QQFDKILATA PVLETAVVQG NIPQEEKWDQ
     QLRFATVQRY LELSEATAAG PEKPPTLIVW PETALPFYPL EHHLFYDIID FAAQHGSCLL
     VGAPHRELDN DRQLQYYNSA MLISPDPAVQ QPAGIYRKQH LVPFGEYIPL RRLLPFFAPV
     VETLGDFTPG PEPALLTCAD RKIGTLICFE AIFPRLARQM TAGGAELLVN ITNDAWFGLS
     NAPHQHLSMA ALRAVENRRS LARAANTGIS VMITPDGRLH QATQLFVPDA RHAALPLPAP
     AGKMNSLFTA GGYLFGLLCL LLLSAGIVRH IYVIKRV
//

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