ID A0A317VKA6_ASPEC Unreviewed; 925 AA.
AC A0A317VKA6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:PWY74784.1};
GN ORFNames=BO83DRAFT_336445 {ECO:0000313|EMBL:PWY74784.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY74784.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY74784.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY74784.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY74784.1}.
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DR EMBL; MSFU01000010; PWY74784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VKA6; -.
DR VEuPathDB; FungiDB:BO83DRAFT_336445; -.
DR OrthoDB; 3149897at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR PANTHER; PTHR24096:SF428; DIDEMETHYLASTERRIQUINONE D SYNTHETASE TDIA-RELATED; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
FT DOMAIN 563..642
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 925 AA; 104035 MW; 056E1A111F79F93E CRC64;
MASGILTYLE QAAEYSPSKG FVFYSVGKDQ PETILYPDFW RLVKRNAQTL VEQKIAVPDR
ILLVHFDTHK ENIIWFWSAI AAGAIPAVST PLAVDPVARE RHLTHLQRLL ERPNVLTSIK
YTDDLSIIDE SQKFFIEDLA SSADQSADYE PANPSSDLAL LLLTSGSTGN AKAVMLHHSQ
IFAAIEAKWK ALASTPENIF LNWIGFDHVA CFMEMHMHAL SRGCHQIHLP AVTVLENPLL
YLEKMAEYSV TNAFAPNFLV ALVGKAIEAQ QERDPRSLDL DLSHLRMVLS GGEANLASTS
ILFNRKLVEM GAAKNVLHPS FGMTETCAGI HYHYSFPELE QKAKLQFCSV GQTTPTLQMR
ITDEHGETVR SGENGNLELH GPMVFKGYYN DDKNTKAAFT EDGWFKTGDT GYIDNRDNLV
LSGRSKDSII INGINFYSHE LENAIDSAGL EGLVPSYTVV VSSWLDNADS EDIIVLYLSS
QKGTEDDRTF LETLNSISRI TALYCSKQPV DIIPLPVELL PKNSLGKLPR TKLKSQYEEG
RFNTYRDLAA QRASAYRARS KRAPQNNMEE TLAGIFADEF DLDVSEVGVD DSLYDMGVNS
VRLIRYKRIV ETRLGLSEEI PMITILQNPT IEALAVMLQD LQKGPKPYNP IVQLQDGPSK
APPIFFFHPG MGEVLVFLNF SKYFADRKVY AFRAPGFNPG EKMFTTIDEM TDTYLKSIRE
LQPEGPYIFI GYSYGAMIAF ETAKKVEASG DRVGFLGSLN LPPHIKKHIR EMDYAESLLH
LVYFLGFITE EDAHRMSPDM HKLPQSEVLP AIMKVSDKER VQELAMDEGK IRDWAMLSSK
LQELAHTYDP SGTVQSMDVF YAIPLLSVGR DKDVWLKQHL MRWKEHSKSV RFHDVPGSHH
TMMAEENVFA LHKILRAALN ERGML
//