ID A0A072PV20_9EURO Unreviewed; 662 AA.
AC A0A072PV20;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase S33 tripeptidyl aminopeptidase-like C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O9_04234 {ECO:0000313|EMBL:KEF59390.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59390.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF59390.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59390.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF59390.1}.
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DR EMBL; AMGV01000003; KEF59390.1; -; Genomic_DNA.
DR RefSeq; XP_013261980.1; XM_013406526.1.
DR AlphaFoldDB; A0A072PV20; -.
DR STRING; 1182545.A0A072PV20; -.
DR GeneID; 25279167; -.
DR VEuPathDB; FungiDB:A1O9_04234; -.
DR HOGENOM; CLU_013364_5_2_1; -.
DR OrthoDB; 1833441at2759; -.
DR Proteomes; UP000027920; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT DOMAIN 304..341
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 523..623
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 662 AA; 73835 MW; 8FEC6AABB57E5965 CRC64;
MDFKSAEMTQ WSPQIRERQK KPRLKLLFCC LTLLLWLFVS IDFSNTFPRL WKGRLLAAEE
TPESATSFQW SQITPSQELE YHDCYGGFEC ARLEVPMDYS APIKATNQVA LAVVRKPAKV
PVSDLHYGGA ILINPGGPGG SGVAQVLDHG ALIQQVVDVE RTPSDAEDSG KYFDIISFDP
RGINRSTPTI SCFQDNFARQ VWNLQSEAEG LLGSSDGSLR LGWRRARALA DGCTSRIDND
NSTSSILEHV NTTPVAADMV EIIERHGQWR ESQGRKAQEA LNKAHKCHGN RDIISRTKWR
RGMEKLQYWG FSYGTLLGAT FASMYPERVS RVVLDGVVST DDYYNGPWLG NLQDTDRILE
RIFEYCDRAG PDGCQFWRPG GGKAIQAAYE KLLHDIWDDP LSVVGNGRRG PEIITWSDIK
DITKNALYQP MIFGPIMVEL LQDITNGTGS LFADYKEKGR VPACRSKQCI LDGPFSEDCI
SPSWNVLEAT SAVLCTDAEG IGSFTEDEFR EYWQTLKAQS WSLGDYWAET RLGCAGWQKH
AKWRFSGPFS ASTSHPILWI GNTLDTVTPL RNAQHMKTLF PGSVLLQQDS EGHCSPTAPS
LCTAKAVRKY FQTGELPLAG TLCKPDIKPF GLQVADGLKR LNAQDSELLD VLMQIARTIP
LP
//
