ID A0A0D7A1A7_9AGAR Unreviewed; 1069 AA.
AC A0A0D7A1A7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Acetyl-CoA synthetase-like protein {ECO:0000313|EMBL:KIY43199.1};
GN ORFNames=FISHEDRAFT_78703 {ECO:0000313|EMBL:KIY43199.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY43199.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY43199.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY43199.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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DR EMBL; KN882115; KIY43199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7A1A7; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT DOMAIN 594..670
FT /note="Polyketide synthase phosphopantetheine-binding"
FT /evidence="ECO:0000259|SMART:SM00823"
SQ SEQUENCE 1069 AA; 118765 MW; B9D8969AD8FF8C0F CRC64;
MPSTPVFGTF KSLFHRPPLD GSLTIPQKYD WHYEHNRDHP VFYFQVGDGR SGVIKDVVLN
YGHLVPAAHQ AGWYVSRMTG VSIQSIGVKK PVIGIMAASD AITLFTTALG VMRAGLLVYL
ISPRNSAVAI AHMLSTMQSR HLILSSEPHI QHLGREAVAE MKTRQGIDLR TSAMPRFEDL
FHCTPENVSS HNIPSFVPLP VRNDDLDSLM AIVHSSGSTG FPKAVVWTSQ MQLQMARLTV
QSKLDWRAEI LAIHGLPMYH IAGFNHITQM PASGMVLGVF CPTNSTKIAT PESCFQGIVD
SSASCAFVVP SHIEAWSKEP SKIKHLLQLK TLAYGSAPID RTVGDHLTQI GVRLCTIYGS
SETALTSDYF PEILGDDWQY FAPNSICKDN IRFRSLGDGT VELIVLSNAS FRTAMTNTVY
NGCDAYATKD VLEPHPSKQG LWRLVGRLDD QIVLSTGEKT NPGPLESILR THPMVKDSII
FGRGHMQNGI LVAPKDEFRF DLQDAKKMKA FLDAIWPRIE QMNAYAPSHS HLSKEMILIE
DPKRPFQFTS KGLPRRSAVL AEYDTDIEAL YAAVEASSAP NINVPTQWTP ESTYDFVKQL
VHSVMRLKVD ADQDFFQYGC DSLQATWIRN AVMKALHSAK VLPQDKELPS NIVYDYPTLD
SLTKVVLQVV SLKPGETVKV FDEKDLLAFV GRYTAELPKE VVLLTGSTGS LGSVVLARLV
AMDSVGKIYA FNRPMSTKTV DIQRDCLKLR EYDENIATSP KIVYVDGTLT VDGMNVRDKL
LEDEIRSSIT HIIHNAWRVD WKVSLNTFQD CVDGVLGLTK FALSSPRQTA PRLLFVSSIA
VLLNYHGEAA LELPVVDPKI PLGQGYGEGK WAAETILNAA RERTRLRPII VRIGQISGGA
NGGWNQSDWV PAIVKSSVTL GCFPMLKGVC SWLGVEDVAG ALIDARNSEH STLHLIHHRP
MAWDVLAQVC ARELSLRLVP YPEWFAKLKT SVEHEVDAAR RKALPAGMLL EFLEANLHRR
DAEGVETFGF THVSVDRMLE VSRTLREVKP IEADDVKLWL SFWRSIGFL
//
