ID   ATP6_ASPAM     STANDARD;      PRT;    78 AA.
AC   P00853;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   25-JAN-2005 (Rel. 46, Last annotation update)
DE   ATP synthase a chain (EC 3.6.3.14) (ATPase protein 6) (Fragment).
GN   Name=atp6;
OS   Aspergillus amstelodami.
OG   Mitochondrion.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; Eurotium.
OX   NCBI_TaxID=5054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lazarus C.M., Kuntzel H.;
RL   Submitted (MAR-1984) to the PIR data bank.
CC   -!- FUNCTION: Key component of the proton channel; it may play a
CC       direct role in the translocation of protons across the membrane.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein. Mitochondrial
CC       inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family.
DR   PIR; A01055; PWAS6M.
DR   InterPro; IPR000568; ATPsynt_Asub.
DR   PROSITE; PS00449; ATPASE_A; PARTIAL.
KW   CF(0); Hydrogen ion transport; Mitochondrion; Transmembrane.
FT   NON_TER      78     78
SQ   SEQUENCE   78 AA;  8736 MW;  139BD9CA17BCFAF0 CRC64;
     MGNLNFVLSP LDQFEVRDLL SINANLLGNF HLSLTNIGLY LTIGIFLILT YSLLATNNNK
     IIPNNWSISQ ESIYATVH
//
ID   AXHA_ASPNG     STANDARD;      PRT;   332 AA.
AC   P79019;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   25-JAN-2005 (Rel. 46, Last annotation update)
DE   Alpha-L-arabinofuranosidase precursor (EC 3.2.1.55) (Arabinoxylan
DE   arabinofuranohydrolase).
GN   Name=axhA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 120.49 / N400;
RX   MEDLINE=97153464; PubMed=9000377;
RA   Gielkens M.M.C., Visser J., de Graaff L.H.;
RT   "Arabinoxylan degradation by fungi: characterization of the
RT   arabinoxylan-arabinofuranohydrolase encoding genes from Aspergillus
RT   niger and Aspergillus tubingensis.";
RL   Curr. Genet. 31:22-29(1997).
CC   -!- FUNCTION: Releases L-arabinose from arabinoxylan.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing alpha-L-
CC       arabinofuranoside residues in alpha-L-arabinosides.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family.
CC   --------------------------------------------------------------------------
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DR   EMBL; Z78011; CAB01409.1; -.
DR   InterPro; IPR005193; Glyco_hydro_62.
DR   Pfam; PF03664; Glyco_hydro_62; 1.
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    332       Alpha-L-arabinofuranosidase.
SQ   SEQUENCE   332 AA;  35837 MW;  F6EEE44EB8C43FEB CRC64;
     MKFLKAKGSL LSSGIYLIAL APFVNAKCAL PSTYSWTSTD ALATPKSGWT ALKDFTDVVS
     NGKHIVYAST TDTQGNYGSM GFGAFSDWSD MASASQTATS FSAVAPTLFY FQPKSIWVLA
     YQWGSSTFTY RTSQDPTNVN GWSSEQALFT GKISGSSTGA IDQTVIGDDT NMYLFFAGDN
     GKIYRSSMSI NDFPGSFGSQ YEEILSGATN DLFEAVQVYT VDGGEGDSKY LMIVEAIGST
     GHRYFRSFTA SSLGGEWTAQ AASEDQPFAG KANSGATWTD DISHGDLVRN NPDQTMTVDP
     CNLQLLYQGH DPNSNSDYNL LPWKPGVLTL KQ
//