(data stored in ACNUC7421 zone)

HOGENOM: PARUW_1_PE400

ID   PARUW_1_PE400                        STANDARD;      PRT;   529 AA.
AC   PARUW_1_PE400; Q6ME75;
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=Putative apolipoprotein N-acyltransferase; (PARUW_1.PE400).
GN   Name=cutE; OrderedLocusNames=pc0400;
OS   CANDIDATUS PROTOCHLAMYDIA AMOEBOPHILA UWE25.
OC   Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae; Candidatus
OC   Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PARUW_1.PE400.
CC       Candidatus Protochlamydia amoebophila UWE25, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:Q6ME75_PARUW
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: HOG000143035 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6ME75; -.
DR   EMBL; BX908798; CAF23124.1; -; Genomic_DNA.
DR   RefSeq; YP_007399.1; NC_005861.1.
DR   ProteinModelPortal; Q6ME75; -.
DR   STRING; Q6ME75; -.
DR   GeneID; 2779648; -.
DR   GenomeReviews; BX908798_GR; pc0400.
DR   KEGG; pcu:pc0400; -.
DR   NMPDR; fig|264201.1.peg.400; -.
DR   eggNOG; COG0815; -.
DR   OMA; GRQFGGF; -.
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; 2.
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; PARUW_1.PE400; -.
KW   apolipoprotein N-acyltransferase;
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Lipoprotein; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   529 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MASIGGFACF WRILLTISSK KERFCLAMGW YAAVQMVQLG WFVSHPYFYI YGVLFFCAWL
     MGAQFGLLAL AIQPSTLKRV SYLFGLAGLW VWLEWSRLFI LSGLSFNPVG IALSGFIYPL
     QFASIGGVYF LSFWVMLTNL WMLRAWFFGW NKREISLAIG CALSPYLMGG SHFYYHLNQM
     NQNTRSISAV LVQPALPIEE NLGFQSAEEA RNFVLQEWHQ ILSTMQKQKG RQIDLIVLPE
     YVVPYGTYHP VFPLENIKKL WKELFGFEAL KSLAPLISPY ASFLSSDRGN QWLVSNAFIV
     KSLANLFQSY VVVGFEDSVY LDEEKTCHAS YSAAFHFSPD QRPAERYEKR ILVPMGEYIP
     FEFCRELAAR YGISGSFTCG KGAKIFNGPV PYGATICYEE TYGDLIRENR QKGAELLVNL
     TNDGWYPNSK LPKQHFDHAR LRTVENGIPL MRACNTGITG AIDSLGQVIN VLGPDMMKTQ
     EIADSLYVQV PVYHYKTLYA KWGDLFILCL SSLLMIWTIA DKFFRCFFF
//

If you have problems or comments...

PBIL Back to PBIL home page