(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7L3_ASPNC

ID   A2Q7L3_ASPNC            Unreviewed;      2396 AA.
AC   A2Q7L3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   SubName: Full=Aspergillus niger contig An01c0050, genomic contig {ECO:0000313|EMBL:CAK43489.1};
DE            EC=2.3.1.- {ECO:0000313|EMBL:CAK43489.1};
GN   ORFNames=An01g01130 {ECO:0000313|EMBL:CAK43489.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43489.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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DR   EMBL; AM269952; CAK43489.1; -; Genomic_DNA.
DR   PaxDb; A2Q7L3; -.
DR   EnsemblFungi; CAK43489; CAK43489; An01g01130.
DR   HOGENOM; HOG000217319; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR032821; KAsynt_C_assoc.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
DR   PRODOM; A2Q7L3.
DR   SWISS-2DPAGE; A2Q7L3.
KW   Acyltransferase {ECO:0000313|EMBL:CAK43489.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphopantetheine {ECO:0000256|PROSITE-ProRule:PRU00258};
KW   Transferase {ECO:0000256|SAAS:SAAS01225069, ECO:0000313|EMBL:CAK43489.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2372..2394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2284..2362
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   MOD_RES         2321
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2396 AA;  262764 MW;  9E3F83BD7D33108F CRC64;
     MQLPDTVAVP GLPVAPAAAQ QTSMPMAVVG IGCRLPGDVS SPAQLWDFLR ECRSGVSEVP
     KDRFNIHSYR GSKDEPGTTL PLGGYFLQDD IRNFDNQFFG INNRDAAVMD PQQRRVLEVV
     FETFESAGVT LDEVSGANVG VYMASFTPDY IAMQTKDPES LTRYSNLGMG ATILGNRISH
     VFNLKGPSCT VDTGCSSSFY ALHLACNALQ NGECDSAIVA GVNLIQSPEL HATVSQGGFL
     SPTSFCHTFD TSADGYARAD GVNAIYIKRL EDAIRNQDAI RSIIRGTAVN SNGRTPGIAQ
     PSIDGQVAVI RKAYARAGLD PAETAYVEAH GTGTKVGDPM EVEALSRVFR KEQRASATLI
     GSVKPNLGHG EASSGLSSLI KATLALEHGQ IPATISVKNI NPKIKTEEWG VDVVTRMTPF
     PLSARGGPNR ISVNSFGYGG ANAHVIIEEA DHKKNQVSIR TGGTGAEIHK TARVSQLPYL
     LPFSANRLQS LKGRVERLSN RDLSCLSVSD LAYTLGQRRS QFACRGYVIT RQETLAQDIT
     VANLQVSTSN LELGSSRLAF VFTGQGAQWQ GMARQLLHYP TFASTIHQLD VELKGLPHAP
     QWKILDIIMD ESDTCPINQA VFAQPITTAV QIGLVALLRS WSILAEGVIG HSSGEIGAAY
     VAGLLSASEA IVLAYYRGYA VTRQASTAGA MAAVGLSSDA AFDWITRLDL ADNVKVACIN
     SPSSVTISGD RGSIEIVVTA LQAKGVFARI LKTDGKAYHS HHMVSVGKLY QSLLDKAGIF
     AKDIVPDTAP LNTHMYSTVI CKPLKRQMAR TTGYWRLNLE SPVRFSEGLK GLSEWIAPNL
     WIEMGPHTAL KLPIIQTLGQ STPYHGTLKR GQDGSVTLLS FLGYLFVHGF RLDFSKLLRS
     YRNESPAKFI YDLPTYAWHY EKPLWNESRT SRESRYRQNP RHELLGTEVP GGSPASFAWR
     NLLHLDHVPW LRDHRLGDTP VFPAAGYTAM AVEALIQKAL PSGTDLTSKR VILRQVALLK
     ALPLKDDDSI ELFTELRPLP ISNVRDSQHW WEFQIFTVLD GSTYTLHAKG MIRLDCGPDG
     TSHAVPSPNC RLTGRSKHVW YDVIARGGLK YYSAFQRIQE VYTPESKGTL YAETSTSSFA
     PEVPTGAQLY PRYFLHPTLL DTVLQLALIA CSGGFHNGLV ARVPTLLGEV SMSLAPHAPG
     ETGIIRAKAS VVGLQKHRAS TYLLNQNQQP VVQFENVEMT AFSAQERTEE VRHPMGRVHR
     KPDITRISED AVFSSALAHV LSVTDLGAFG SRSRLLAALD MIVHKKPDSR ILCLAXDLSF
     VALACLEVLE APVVYRRFET FSLGRIGPDG ALEVAEVRNY TVPLGLGSMA YRKATSDDQY
     GVCILGQGTS QAVVGHLKKH TNECTFFLGP CTQFPAPVPS SHLQLTDRDH GVHVLRPNPK
     FTSQFNHVLL VEASFMDSKL ASHLSKELDM PVQALTLRDI PHSPILPQTL VVSVLELHKS
     LLSDPTAEEY DAIKKVIEHA AHIFWISGSG VHNGFDPTRS IFTGLARALI VEQPSTRIFS
     LEIDPATEMS VVSRDVCQIL QQKNEVDYEY IRDGSQLLIS RVVPDERLNR EFRRRHNSIP
     MPKPLAQVDN AYLLVPEPGQ LNSARFVQRP SSPTLPADHV LVKVACMGLN AKDVYVMAGR
     VSTKNATCSS EFTGQIVELG ADVQSFKVGD RVAVMHNGHF GTYETVPWWS CIRLEEHEDL
     VSMAGVLVVF FTAVYALEYR ARLEPGESLL IHSAAGAVGI ATIQLAQHLG VGDIYATVGN
     EEKKRYLVEH FGLRSENIFS SHDTRFAEKI KVQTRGRGVN VILNSLVGDL LHESWDCLAD
     WGRFVEIGKR DILDCGKLNM STFARGTTFT SFDLNMLNEL DTPEAARQLK RTILARLLQL
     VRAGHVQPVQ PLAVFPVSEL SAACNHFNNA KRMGKIVISF EDQTQIVPTV PVLYSTVLNP
     NKSYLMVGCL GGLGRSLSRW MMNRGARHFI FLSRTGLAKP AARHFVQELK QAGARCTIVT
     GDVTTYEDVE RAVAAAVADA PLGGVIQAAM GLHEAIFSHM PREYWLTGTQ AKVRGTWNIH
     QALGKLKCES ALDFLLLTSS VTGQIGMATE GNYCAANHFL DVFARYRQSL GLRAISLGLG
     TISEVGYLHE HSEIGELLLR KGIRPLPENE VLQIVDFALS SDIDQQQTVP RDRLAQCHIL
     TGIEDTKLQD HRKQGFTGFW HNLDNTRFSV LINALQRQAS QSESGINTPA SVIQTVLASG
     DEKQLREAVI QAIAKKMSNI ILLPLPKLDL KLPLSDYGMD SMLSAELRQY IFNSMGVDVP
     FLTLMDTATS VLSVAEMVLE ELGKIIRNKN NIMIYAIIIL PKLSAILALV DYLISL
//

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