ID A0A0A2VYU4_BEABA Unreviewed; 824 AA.
AC A0A0A2VYU4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Protein amidase {ECO:0000313|EMBL:KGQ05924.1};
GN ORFNames=BBAD15_g8827 {ECO:0000313|EMBL:KGQ05924.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05924.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05924.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05924.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ05924.1}.
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DR EMBL; ANFO01000904; KGQ05924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VYU4; -.
DR STRING; 1245745.A0A0A2VYU4; -.
DR HOGENOM; CLU_009170_0_0_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07566; ScNTA1_like; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039703; Nta1.
DR PANTHER; PTHR11750; PROTEIN N-TERMINAL AMIDASE; 1.
DR PANTHER; PTHR11750:SF26; PROTEIN N-TERMINAL AMIDASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT DOMAIN 1..280
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 289..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 92797 MW; DAC7EA344A3CACDC CRC64;
MRIACLQFAP QLAAIEGNVE RADAILSRAD PQDIDLLVLP ELAFSGYNFK SLGQISPHLE
LGEFGITAAW SRQVALKYDC AVIAGYPEKI DPVHSWPADP EYYNSAIIID GDGSVVGNYR
KSHLYYTDET WALEGRDGFF TGHVRGLGQL VVGICMDINP YRFEAPWEAF EFSSHALQAG
ARLIVLSMAW CTNADLQEFC LKPDEPDMDT LLYWITRLQP IISIDFNQET IIVFGNRCGA
EGDTTYVGTS TVIGVKSGEI FLYGILGRGE ESLLVVDTDA QPYAKIKLQS SESVQAQDQI
EDDPASQSYP QTDPADKQRN PRGSEICAKK GTEPNQATTT DVREHTLDTI RVTREEEGNS
HYDHDWLEPS RRPREHPTSG PFRVDGSSVG LASSSSHISY TQFTQSHVAA PATQQHDMGE
MRPTMSDGDY HRNRMDDFSE SDDELLLYDS CAESEEEGWP YPQESQLRDA ERYRGAASTQ
REHGAQNAGK RLPTIHRLQP GLPSPLSEQD VISQSSLVHR IASFALAHQV SPTPNTENFR
EEDIYRHVHG KNLTSEHHIR YHTRLLRERL ARQGLSAEAT DDEEEDLEES QEEYHEREEN
EVDFVPHKDP DKLHHAGRRT LELASPTRVR AGLETQPNYT HESVSQARQP VWLEHPAEPT
PIVDSPMSHM TLFSPTRTRR RHARQAPAYA TAVPGRAGAV AIESGMDLDE RAVHQARLPV
LGRSKAKENS IPLLDPSRRP KAAARQVPPL RLVPREAPQE REREVRERSR RIPRQLPNTR
EMEGPMPRDN GGDNDRDRGR KTPVPMVLVY EGEDEYVPLR SRRS
//