ID A0A166VYI9_9HYPO Unreviewed; 1046 AA.
AC A0A166VYI9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Male sterility, NAD-binding protein {ECO:0000313|EMBL:OAA34168.1};
GN ORFNames=BBO_09308 {ECO:0000313|EMBL:OAA34168.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA34168.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA34168.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA34168.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA34168.1}.
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DR EMBL; AZHA01000062; OAA34168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166VYI9; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0044249; P:cellular 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 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 SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
FT DOMAIN 23..342
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 684..919
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 1046 AA; 115153 MW; 4C345F9DD5B7D8FC CRC64;
MTVNGHTPYG GPYGRRLYVN VVDETANADP DRTWIYAPRS SDPRDGWKAI TWQQHANAVN
RTANWLVEKL GKPEPKSFPS LAYVGPNDAR YLILFAAGVK AGYQIMFPSP RNNTDSQVSL
LQVTKCQKLL YGKEYAKRIQ PWLHESGIGA LEMLGLDQAL KDEAAPVHPY NETFKSAEFD
PVVILHTSGS TGVPKPIYCK QGLFAAADNY HNFLEYEGFE FMMEAVAAYS KNTYCPLPLF
HAFGLYCFVN ITVFWGKPMS LAIGDKPLTA KSVVEGYEAA GSDALILPPS IVEDLAKLDG
GVERLKQLSY VGCGGGGISP EIANDITSKG VKLMNCISST EYQLYPLYWQ KNYQNWDWFI
FDNEQFGCRY DHVEDNIYEQ TIVRKEPFQP IFYTFPDATE YKTGDLYEKH PTLPGHWRSQ
GRVDNIIVFS NGEKLNPVSI ESTVTLHPDI RQALVVGHGH FQAGMILEPA QWPLDSAQKE
ALIEKVWPVI EKANAATVEH GRIARHLVTL SDPEKPFLYS AKGSLRRGAV IKMYKKDIET
LFSAQEVIKP AQLNTATLES LTASVRSLFN SVSPGGTIED EDDFFLHGID SLQVINIAKR
IAAGLKAAGV AEDRAVLAPR DIYAESTISK LTSFLFSRIH GTQSNGAHSQ EEILQALVDK
YSADLAKRSD TRPPAKSTGK TVLLTGSTGS LGSYFLHFLI QDPEVAKVVC LNRSQDGGRA
KQLEANKERG LSTDLDRVAF FHADLSRPDL ALEAHDLVRL QESVDLIIHN AWPVNFNISV
QSFEGHIRGV RHLIDFVQNT AVKASITFVS SIGTVDKRSD ASAVPETNLT DLNLAAMGYG
QSKQVSSIVL DTAAKVAGVP AAVVRLGQVA GPTTRLGSWN AHEWLPTIID SSVQLGSLPD
TLGSMQVDWV PVDKVARTIL DMAAYTTKAT DFTSGAKFFN LVNPKTTPWS TIAPAVVDFY
EQGGKRLQLV SFAEWIKAVE DAPASFKLPA IKLLDSYKAM DEGAKNGSIS SFATDKAQLA
SKTLASMEAI TPELMALWCK QWNFST
//
