ID   A0A0B7MTL0_9FUNG        Unreviewed;       452 AA.
AC   A0A0B7MTL0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF00561};
GN   Name=PARPA_02885.1 scaffold 5990 {ECO:0000313|EMBL:CEP09391.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP09391.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP09391.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP09391.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC       {ECO:0000256|ARBA:ARBA00006886}.
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DR   EMBL; LN721622; CEP09391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7MTL0; -.
DR   STRING; 35722.A0A0B7MTL0; -.
DR   OrthoDB; 2600616at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   HAMAP; MF_00296; MetX_acyltransf; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR008220; HAT_MetX-like.
DR   NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR   PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          66..397
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   REGION          250..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000443-1"
SQ   SEQUENCE   452 AA;  50374 MW;  69BF7574F5315581 CRC64;
     MQEYKTFATL KELPFEESKN KLVKLIPDQN ITIIPEYTLE SGVKLTSIPI AWKTWGKLND
     KADNCMVICH ALTGSADVED WWGPLMGPRR AFDYTKFFIV CCNVLGSPYG SASPLTVNPE
     TGNIYGPEFP LVSVRDDVAL HRLILDQLGV KQIAVCVGGS MGGMQVLEWA QMGQDYVRTI
     VPIATSGRHS AWGISWGEAQ RQSIYSDPNY ADGYYTDSAP PNVGLSAARM SALLTYRSRN
     SFESRFGRKA ADMKPVNRPN SPREANRLIH NDGHRETSPA ESSANEAKIG TINNPTMPTP
     FVFSAQSYLR YQGNKFINRF DANCYIALTR KMDSHDLSRG RGDYFDILAS IDQPALVIGI
     ESDGLFTISE QYELAEGMAD TEMIVIDSPD GHDGFLLEFD QINRHLLSFI KRVVPEIYSS
     TTITDEELEQ SEVVKATKTS LFGEAEVDIT QW
//