ID Q6BQZ8_DEBHA Unreviewed; 340 AA. AC Q6BQZ8; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 81. DE SubName: Full=DEHA2E01078p {ECO:0000313|EMBL:CAG87575.2}; GN OrderedLocusNames=DEHA2E01078g {ECO:0000313|EMBL:CAG87575.2}; OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Debaryomyces. OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG87575.2, ECO:0000313|Proteomes:UP000000599}; RN [1] {ECO:0000313|EMBL:CAG87575.2, ECO:0000313|Proteomes:UP000000599} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC RC 2968 {ECO:0000313|Proteomes:UP000000599}; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L., RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC {ECO:0000256|ARBA:ARBA00038310}. 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; CR382137; CAG87575.2; -; Genomic_DNA. DR RefSeq; XP_459372.2; XM_459372.1. DR AlphaFoldDB; Q6BQZ8; -. DR STRING; 284592.Q6BQZ8; -. DR GeneID; 2902920; -. DR KEGG; dha:DEHA2E01078g; -. DR VEuPathDB; FungiDB:DEHA2E01078g; -. DR eggNOG; ENOG502RZT7; Eukaryota. DR HOGENOM; CLU_044590_1_0_1; -. DR InParanoid; Q6BQZ8; -. DR OMA; IAWRTAM; -. DR OrthoDB; 1348533at2759; -. DR BioCyc; MetaCyc:MONOMER-16238; -. DR Proteomes; UP000000599; Chromosome E. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR032466; Metal_Hydrolase. DR PANTHER; PTHR43569; AMIDOHYDROLASE; 1. DR PANTHER; PTHR43569:SF2; AMIDOHYDROLASE-RELATED DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF04909; Amidohydro_2; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000000599}. FT DOMAIN 185..338 FT /note="Amidohydrolase-related" FT /evidence="ECO:0000259|Pfam:PF04909" SQ SEQUENCE 340 AA; 40004 MW; 3A12FBCD17FC1ED4 CRC64; MPSKKYKIID SHVHLFAKRN FKLLKFDEAH PLHSDFRLDE YLKYSMNEEF QIDGLVFIET DPIADLSKAL EGCEYPIQEY LYVARNITGN LLPDEGETSE LKQNFIKAIV PWAPMPLGKS SVSSYVEMLK SRSSTDEFNL VKGFRYLVQD KLPNTMLQRD FVESLKWLDD NNFIFDWGID LRCGGLWQFE ETIEVLKQVP NLKYVINHLT KPNLSIDPTK IEENDEFLQW KNYMKQIFVN SPNSYMKLSG GFSELPSEII ENRDKCAEYI YPWFKVCFDL WNVDRTIWAS NWPVCTLTAG EDLTSKWFEV TEMLFDKIEL NEESRKKIYG TNYLKAYNLI //