ID A2RAH5_ASPNC Unreviewed; 1197 AA.
AC A2RAH5;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Contig An18c0080, genomic contig {ECO:0000313|EMBL:CAK48701.1};
GN ORFNames=An18g03170 {ECO:0000313|EMBL:CAK48701.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK48701.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK48701.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {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; AM270401; CAK48701.1; -; Genomic_DNA.
DR RefSeq; XP_001398777.1; XM_001398740.2.
DR AlphaFoldDB; A2RAH5; -.
DR EnsemblFungi; CAK48701; CAK48701; An18g03170.
DR GeneID; 4989879; -.
DR KEGG; ang:An18g03170; -.
DR VEuPathDB; FungiDB:An18g03170; -.
DR HOGENOM; CLU_005444_1_0_1; -.
DR OrthoDB; 1005457at2759; -.
DR Proteomes; UP000006706; Chromosome 8L.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd08606; GDPD_YPL110cp_fungi; 1.
DR CDD; cd14484; SPX_GDE1_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF1; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE GPCPD1; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51382; SPX; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..144
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 458..490
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 491..523
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 529..561
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 812..1139
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 591..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1197 AA; 131311 MW; 53C8C7CA6F425C17 CRC64;
MKFGRQLPRN VVPEWGSEYI KYKALKKLIK AAADNVKAGK EADLAGFFYS LDRNLEDVDH
FYNKKYADFS RRLKLLEDRY GQSLDGGQRL DSEDVEDLLA ALLELRSQMR KLQWYGELNR
QGFIKITKKL DKKVGAQAQQ KYLQTKVDPA PFASNTRVTD ALRKINDRLS VLGEQKIDDD
ASSIRSSLSL KKGPARPNLN LPASMLQTVD EALRKDDTHV LLELLVTLKA AADESGEDVY
PKVLNSLLQR SINYRSTSCI SVLLGRMDSL DEEDDINRRN CIHRLVISIG RAQSTTDSEQ
SASMVLDFPL ETSNYITPAA LPTLQPPRPV VMEADHPSHL DRSDPSVSLL QYLLDQLLPN
QRGALVAKDI AGRTPLHYAA QYGFKVVCEV IIEHLQAWDL FDVTEGIDGP RWQDNDGWAP
LHLSVVGGHP LTTRALLEAE NWHGANKDKA KIRKQVSRSS AVLALATKAN FVDIVKLLVE
AGVDINYQDE QGETALHVAA RFGHDKCAKI LLDGNSEQKA DTELAENTYS WTPLFIACVD
GALRVVELLI EAGANLERCD SSGWTAKEHA SLRGHLDIAR CLAKVTPAPD ISESEPVIPV
PPVASDPPSP PLSSLAERRS NGTPAASSLR NAEPIKTFGH RYLTDESMVL VSLGTMDMRT
HTAAVNLDRI PMENAHSTQL DTALSLVVSA SRARGEPEVI DLPVQENIST EPIVFHAADA
TKVRLLFDLI PTYAGSKDKV VGRGVALLSS IKQSVGSNRI NLKGDSTVPI VAANTLEVIG
SVTFNFLIIT PFKHPNMTVT GEQTYWRSMS STMVIGHRGL GKNMASRNSL QLGENTVQSF
IAAANLGASY VEFDVQLTKD HVPVIYHDFL VSETGIDAPV HTLTLEQFLQ LGDKGPSRRP
GSPVPGTDGI GEGMAAAFRQ RSMSVGGSEY DPTELNEKIK HTRDFKKKGF KGNSRGNHIQ
APFATLAELF QKLPKSVGFN IELKYPMLHE SEEEEMDTYA VELNSFVDTV LTKVYDMGQG
RNMIFSSFNP DICLLLSFKQ PSIPVLFLTD SGASPVGDIR ASSLQEAIRF ASRWNLLGVV
SQAEALVLCP RLVRVVKESG LVCVSYGAIN NDPESVKLQV AEGIDAVIVD SVLAIRKGLT
EHQGKGDTPG VSPQPSPLAR ATSGSLKESL NIPVLNQTEQ KDDHLHVKPE AITSNPR
//
