(data stored in ACNUC7421 zone)

HOGENOM: DINSH_2_PE20

ID   DINSH_2_PE20                         STANDARD;      PRT;   523 AA.
AC   DINSH_2_PE20; A8LSX9;
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   RecName: Full=Apolipoprotein N-acyltransferase 2; Short=ALP
DE   N-acyltransferase 2; EC=2.3.1 -; (DINSH_2.PE20).
GN   Name=lnt2; OrderedLocusNames=Dshi_3613, Dshi_3951;
OS   DINOROSEOBACTER SHIBAE DFL 12.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DINSH_2.PE20.
CC       Dinoroseobacter shibae DFL 12 plasmid pDSHI01, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A8LSX9_DINSH
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   -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N-
CC       acyltransferase subfamily.
CC   -!- SIMILARITY: Contains 1 CN hydrolase domain.
CC   -!- GENE_FAMILY: HOG000264280 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8LSX9; -.
DR   EMBL; CP000831; ABV95346.1; -; Genomic_DNA.
DR   EMBL; CP000833; ABV95679.1; -; Genomic_DNA.
DR   RefSeq; YP_001541827.1; NC_009955.1.
DR   RefSeq; YP_001542160.1; NC_009957.1.
DR   ProteinModelPortal; A8LSX9; -.
DR   STRING; A8LSX9; -.
DR   GeneID; 5714143; -.
DR   GeneID; 5714480; -.
DR   GenomeReviews; CP000831_GR; Dshi_3613.
DR   GenomeReviews; CP000833_GR; Dshi_3951.
DR   KEGG; dsh:Dshi_3613; -.
DR   KEGG; dsh:Dshi_3951; -.
DR   OMA; GNVEQSQ; -.
DR   ProtClustDB; CLSK983467; -.
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; DINSH_2.PE20; -.
KW   apolipoprotein N-acyltransferase;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Lipoprotein; Membrane; Plasmid;
KW   Transferase; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   523 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKPGLPQFVS EDLNLFQRMG LALAAGGLTV LTLPPFSWLI AVPVAFSVLF IVLRNISTSR
     AFLVGWAFGL GQFGIGISWI AESFYVDAER FGALAIPAVA GLSAGLAIFP GMAAMLFAAI
     MQRRAVGGIA AGLLFATCWV ATEWLRGHVL TGFPWNLAAY ALVDYAALRQ PAAWVGSYGL
     GFLTVFIGIL PGVLTVAAPK RRAPVLVLFA VAVAGFWVGG ALRSGQDVPP TDVALRIVQG
     NVPQVEKWVP GSRQRTLEKY LGLSAQPGRF DLLLWPETAF PGFLDEDAAA RARISAALPD
     GRILLTGAPD RVEGDGGTRY FNTVQAYDGS GEVLTGYAKH HLVPFGEYVP LKGWLPIERL
     TEGLGDFTPG PGPRTLAIPG APLVAVAICY EIIFPGHVVD DLFRPDWIFN ATNDAWFGTS
     IGPEQHLASA RMRAVEEGLP VVRAANTGIS AIIDANGNVV ARLDTGETGT IDAGLPGART
     PTPYARFGDW TLLVLVFGCW VFGWLASLLG RDPDARHFGT EVS
//

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