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Database: UniProt
Entry: B8M7N8_TALSN
LinkDB: B8M7N8_TALSN
Original site: B8M7N8_TALSN 
ID   B8M7N8_TALSN            Unreviewed;       703 AA.
AC   B8M7N8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Amidase, putative {ECO:0000313|EMBL:EED19591.1};
DE            EC=6.3.4.6 {ECO:0000313|EMBL:EED19591.1};
GN   ORFNames=TSTA_028730 {ECO:0000313|EMBL:EED19591.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED19591.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- SIMILARITY: Belongs to the isochorismatase family.
CC       {ECO:0000256|ARBA:ARBA00006336}.
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DR   EMBL; EQ962654; EED19591.1; -; Genomic_DNA.
DR   RefSeq; XP_002480025.1; XM_002479980.1.
DR   AlphaFoldDB; B8M7N8; -.
DR   STRING; 441959.B8M7N8; -.
DR   GeneID; 8098992; -.
DR   VEuPathDB; FungiDB:TSTA_028730; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_025343_0_0_1; -.
DR   InParanoid; B8M7N8; -.
DR   OMA; VECCVTT; -.
DR   OrthoDB; 5490475at2759; -.
DR   PhylomeDB; B8M7N8; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd00431; cysteine_hydrolases; 1.
DR   Gene3D; 1.20.58.1700; -; 1.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   PANTHER; PTHR11895:SF169; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EED19591.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN          37..226
FT                   /note="Isochorismatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00857"
FT   DOMAIN          281..686
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   703 AA;  75483 MW;  CF627D54E5EAF7CB CRC64;
     MAATLSIKRI PSGAEDSEVV SFEAQPYAFQ FDPSAAALVI IDMQRDFLLK DGFGYIQAGD
     AGVEKVQATI KPTLEVLRKF RERGIHVIHT REGHRPDLRD LPTPKLLRQA RAPNTRHSMV
     IGDLGPMGRL LTRGEYGHDI IDELQPVAGE FVIDKPGKGS FFSTTLHEHL VDRGITHLIV
     AGVTVECCVT TTVREANDRG FDACILRDCT DGFVSTFKSA SLDMIHFSEG LFGFVSESQP
     LLAALSSFPP HPKNLALDWD GSMSIEALKN AYSSGLSPVT VVRHVLKKIS ADKPQHSAVW
     LSLASSKNLL GRAEDLERSG DCNLPLFGVP FAVKDNIDVS GLPTTAACPG FEYVPEKSAF
     VVTKLEAAGA IVIGKTNLDQ FATGLVGTRS PYGACYCTFS PRHISGGSSS GSAVAVALGH
     VSFALGTDTA GSGRIPASFN NIVGLKPTKG TVSTAGVLPA CRTLDCVSFF ASTISDARIA
     WLAAKAHDPE DPYARSSPSL ASLNSRSVLH GDALSPAYQE QFAKVLSLVR GLANIEEVNF
     DWSAYLAASD LLYKSALVTE RTAAVQELLG SKAKRISLHP VTQKVLDSAS SKTATDVFRD
     VHKAQRLLKV IEAEFDKCDI LVVPTAPNHP TVAEVEQDPI VPNLKLGIFA SAVNILDLAA
     VAIPAEHIDG LPFGISIIAP AFREGFILKV AERIRKRMEH FVL
//
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