ID A0A2V1C0W1_9HELO Unreviewed; 501 AA.
AC A0A2V1C0W1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:PVH79340.1};
GN ORFNames=DL98DRAFT_516117 {ECO:0000313|EMBL:PVH79340.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH79340.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH79340.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH79340.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; KZ804155; PVH79340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1C0W1; -.
DR STRING; 1485229.A0A2V1C0W1; -.
DR Proteomes; UP000244409; 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:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 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, ECO:0000313|EMBL:PVH79340.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..501
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015968150"
FT DOMAIN 85..245
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 402..498
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 501 AA; 53589 MW; 406C340C6F6FC64C CRC64;
MQQFFCFSHI SATLILFSQA LALPHIPPRT NPKISWGNCT ASDPPNLQCG QIEVPVDYDN
PRGDQFNVTF ARLQTLNATS RIGSLIFNPG GPGGAGSDVV FAQIQGAPFF SPELLAQYDV
IGLDPRGTGL SNPIVCDPEI WNQRVSSTPK NEEEFNKLVE YNKAFSESCK AGTGPVFDFM
GTTSAARDMD MVRRALQEDK LNFLGMSYGS NLGSTYAGLF PTKVGRMVLD GILAISDSDT
SLLATESETY EATLNQFFKW CNTTSDCALS GQDAPGIFDN IIASANEKPI PAPGCTVGNV
SVCRSDATGE EILSRVQLGL LIVEQSVLSA GWSGLSVAIA EAAQGNATLL SVPIKSAPSD
SDFSFLGVAC KDWVPTSKSH IDLAFKRQMT NALSPHSRGS SQTYQAQSSC IGWASPPTPG
QSLRPKQVAK LPKILLANSF WDPSTSIVWA NTLKQEVPSS VLVLRNGSGH TSYFGHGKIS
KAMDTFLLTG ESPAQGTVFD S
//
