ID A0A4U6XL95_9PEZI Unreviewed; 744 AA.
AC A0A4U6XL95;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 05-FEB-2025, entry version 11.
DE SubName: Full=Alanine--anticapsin ligase {ECO:0000313|EMBL:TKW56384.1};
GN Name=bacD {ECO:0000313|EMBL:TKW56384.1};
GN ORFNames=CTA1_7200 {ECO:0000313|EMBL:TKW56384.1};
OS Colletotrichum tanaceti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=1306861 {ECO:0000313|EMBL:TKW56384.1, ECO:0000313|Proteomes:UP000310108};
RN [1] {ECO:0000313|EMBL:TKW56384.1, ECO:0000313|Proteomes:UP000310108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP57314 {ECO:0000313|EMBL:TKW56384.1};
RX PubMed=31150449; DOI=10.1371/journal.pone.0212248;
RA Lelwala R.V., Korhonen P.K., Young N.D., Scott J.B., Ades P.A.,
RA Gasser R.B., Taylor P.W.J.;
RT "Comparative genome analysis indicates high evolutionary potential of
RT pathogenicity genes in Colletotrichum tanaceti.";
RL PLoS ONE 14:e0212248-e0212248(2019).
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:TKW56384.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PJEX01000070; TKW56384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6XL95; -.
DR STRING; 1306861.A0A4U6XL95; -.
DR OrthoDB; 434648at2759; -.
DR Proteomes; UP000310108; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR052032; ATP-dep_AA_Ligase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR041472; BL00235/CARNS1_N.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF18130; ATPgrasp_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:TKW56384.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000310108}.
FT DOMAIN 369..625
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 487..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 80380 MW; D9424F1AECB5E6B4 CRC64;
MPQSDSISTR NVNAAHLGGT EEFDAIVAGN RVFFRCHWKL NGQPKAVQDL DPDDNVNRSL
QPPCRTLDLV LIAISVMPQY GKAASGLSSS AGDENRGIGG FLWGPPDAAA AAAVDSAARR
FIRAAVDRNI AQYASSITAV KLVLPTVDGY ALRNDLVQRR LLTCDLVEEA ADFTSTGREI
HAFDWDEGGG TRVIIPRALD GAVGAVLQKQ LPSMQLQLVE YTLSLLEAEV AGRLSFPWIS
RSPLPRFRLA VVEARPNEMV AATAGMGMYR AARALGIDLV ILERDHGWAR KLAATEEGGG
VSVEFVPCDL TQDDGLPDRI VEALSHGRRP AVDGITTFND YYTHVTALVA EKMGLPTNPS
QSIHLCRDKA KMRQAVCPDT QVLSVQGLAD LRQTLSGLKT PLQYPLIVKP AIGCASEGVT
RVSSEADLFM AVDRIEHKFP GTSSLLEPYA SGPEVDVNLM FLDGKLIWGE VVDDFPTSAE
VDEVAGHNAS GAPKSNRGAG AGAEPQTPSS SISFAETSDI LPSILPSDEV DLLKRDLAEK
LKRLGIRNGL FHLEARVENS KARFAMTHRG VEVVPREDST STGNEPDPSV FLIEINARIP
GHQESYSVEY TYGIDYYALQ LLAALVPPGE GESAARDVVK THIRALSRPL QPNSQFPTHI
VFSVATRGGT FLGADPLPAS LARWITNSKV YKNVGDVIGD PSVEGKWPFL AYFGVTGRWP
GRDGREQARG LGELVRETFT CSVE
//
