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Database: UniProt
Entry: B8MFI4_TALSN
LinkDB: B8MFI4_TALSN
Original site: B8MFI4_TALSN 
ID   B8MFI4_TALSN            Unreviewed;       509 AA.
AC   B8MFI4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Alpha/beta hydrolase, putative {ECO:0000313|EMBL:EED16718.1};
GN   ORFNames=TSTA_017920 {ECO:0000313|EMBL:EED16718.1};
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:EED16718.1, 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 peptidase S33 family. ABHD4/ABHD5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038097}.
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DR   EMBL; EQ962656; EED16718.1; -; Genomic_DNA.
DR   RefSeq; XP_002483952.1; XM_002483907.1.
DR   AlphaFoldDB; B8MFI4; -.
DR   STRING; 441959.B8MFI4; -.
DR   ESTHER; talsn-b8mfi4; CGI-58_ABHD5_ABHD4.
DR   GeneID; 8109992; -.
DR   VEuPathDB; FungiDB:TSTA_017920; -.
DR   eggNOG; KOG4409; Eukaryota.
DR   HOGENOM; CLU_017361_3_0_1; -.
DR   InParanoid; B8MFI4; -.
DR   OMA; HLYLDGW; -.
DR   OrthoDB; 276964at2759; -.
DR   PhylomeDB; B8MFI4; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   PANTHER; PTHR42886:SF29; PUMMELIG, ISOFORM A; 1.
DR   PANTHER; PTHR42886; RE40534P-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EED16718.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN          156..280
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  56647 MW;  A28C949DA50325C4 CRC64;
     MPSVETVSQA HGGMGNEGLQ DTRESGRKLP HSVTHGMAPA SSSWLPLGMK ETLHQWWHKA
     PAAVAEHKVL STIPYLQEAP TQLQTGSTAS APNSPTATDS LQAVDPSQSG DEIVNSNNDP
     YGPRRWRSRM VELSGKNRAL NEFSVERIGE EADQNLVMLH GYGAGLGFFY RNFEPLSRAK
     GWHLYALDLL GMGRSTRPPF KIKASDREEA ITEAENWFID ALEEWRVKRK IDRFTLMGHS
     MGGYIAAAYA LKYPGRLNKL ILVSPVGIPE DPYAVNEAMP TDSTEGNGTN NRMPPRLPRL
     ITYLWDANVS PFSFIRWSGP LGPGLVSRWT SRRFSHLPYA EAAALHDYTY SIFRLRGSGE
     YALTYLLAPG AFARSPLIRR IQGIGRQVIR PDSPVAMTSV SDVSAASVAA SPASQPLREN
     GIPVIFMYGD HDWMDVAGGF SAKEKIEEER RRILKEATPE QREADNGSAK VYIVKNAGHH
     LYLEGDEEFN DIILKEMEDV RRREAKRQS
//
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