ID B6QEJ0_TALMQ Unreviewed; 658 AA.
AC B6QEJ0;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Proteinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PMAA_089350 {ECO:0000313|EMBL:EEA24964.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA24964.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
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.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; DS995901; EEA24964.1; -; Genomic_DNA.
DR RefSeq; XP_002148475.1; XM_002148439.1.
DR AlphaFoldDB; B6QEJ0; -.
DR STRING; 441960.B6QEJ0; -.
DR VEuPathDB; FungiDB:PMAA_089350; -.
DR HOGENOM; CLU_013364_5_2_1; -.
DR OrthoDB; 1833441at2759; -.
DR PhylomeDB; B6QEJ0; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF25; PEPTIDASE S33 TRIPEPTIDYL AMINOPEPTIDASE-LIKE C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..341
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 541..613
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 658 AA; 73211 MW; B167E5EE7B0B143E CRC64;
MGFVQKQPEG PPRGKQFSRI RVLLVSCVFA LAVLFNVQQW IFPAQIKEDE QTQSILDEPS
EFAWHYITPT TNLKYYPCFG KYQCARLELP MNWNRTDGGG EKIALAIIKL PARVPVTDKR
YGGPILTNPG GPGGSGVSFL FGRGQQIQSI VDFTTDQPEA DSELGKYFDI ISFDPRGVNN
TTPTWSCYPD AQSRYEARLQ EEAEGIIGSS DNAIHQAWAR NMAFGAGCAK SKSGPEWLGN
FMNTSPVVLD MVEFIERHGE WREAETERLL SQKTHQLSSS DAVEAVRRRN IWKRGEEKLL
YWGFSYGSVL GMTFAAMEPH RIGRAAIDAV CNATDYYTGS WLSNLQNTDA VMDKFFEYCH
EAGPEGCPFA IGQTAKELKE KFEDILASLK KEPIMVLGTS DQAPDVVTYS DLNRLVAETV
YFPYQYFELL AKVLAEAAQR NGTSLLEVKR QGHKSWLPSS SDCEKDASGK DCHSVDHEAG
IGIAGTDVLN VKNISKASFF EYRETLNNQS KVLGDMWSSI ALSYLGFKER PAWRFDGEIG
GQTAHPLLFI GNTRDPVTPL SNAHLMSGFF PNSAVLEQRS EGHGSISAPS LCTAKNVRRY
FQNGELPSTG TVCEVDELPF HLGQGSYQDQ SLSSADEDML RTALRTLSRE PSVFKPLF
//
