ID A0A423X6J5_9PEZI Unreviewed; 823 AA.
AC A0A423X6J5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_01298 {ECO:0000313|EMBL:ROW11545.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW11545.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW11545.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW11545.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROW11545.1}.
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DR EMBL; LKEA01000002; ROW11545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X6J5; -.
DR STRING; 356882.A0A423X6J5; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR CDD; cd06121; cupin_YML079wp; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR009327; Cupin_DUF985.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR039935; YML079W-like.
DR PANTHER; PTHR33387:SF3; CUPIN_5 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33387; RMLC-LIKE JELLY ROLL FOLD PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR Pfam; PF06172; Cupin_5; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000283895};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..823
FT /note="AB hydrolase-1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019240215"
FT DOMAIN 46..178
FT /note="DUF985"
FT /evidence="ECO:0000259|Pfam:PF06172"
FT DOMAIN 329..511
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 687..771
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 316..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 90869 MW; 24B256820B677939 CRC64;
MPSLSRYSTC FLGLLTLMVG PDAVFSRPSS TGTQIRPISV NDRPAQDIID KLNLIPNDEK
GYYIQGFEDP YTIPCLNQSA STAIYYLLQG TDGESVWHRV DAAEVWHYYA GAPLVLSLSY
DNGQPLRNKT LGPDIFNNQQ PQVAIQKGEW QRARSLGDWT LVGTTVAPGF VASGVELADP
GLVGLVLVSK WTASRYVRDC HHYHDPQVTG GIYGRFPQSN DAFNFLPCTN ATLPPSLDDE
DHKASWSNLF DPDPDHWSWG NRTDPAVATG DPYAGRGIYL CGYIDVPLDY HNESDTRIVR
LAVTKFQVSG LARVDGSSAP GAGNKSERTL VLEPGGPGGS GTRMVWGSGE ELTNRLTEHT
FDALGWDPRG VNTSQPAIAC YPYSADRDRW SMLAGQYREV SDPDQQLRVM DAMNNATFYA
CWKRFGDLGR FMTTALVARD LEEIRKGLGE DELTGYLVSY GTGIGQTYAN MFPESVGRMI
LDGTEYVRDH RLLGGFGWTA LDNVTNAWHD GFLGECLNAG PEHCALAKPL GGKPVDLMHL
EARMETLVTS IIENPIPGYT ETGGPSLITY SGLVSAIYGS LYNAKSWPAT AEMLYELEAG
NSTLAAAFLE RMLWEYDPTH PQPPSPRPLT DELTYLVICA DAYDAPMPLD GLTWWSSLWA
NMTAKSWISG NSRFTNVFPC RHFTTYWPDV AEVYRGDLNN TLRHPVLLIA ETYDPATPLR
NGRRLAAEMG ANAVLIAHHG YGHSSRDASN CTDSIARAYI LNGTVPEEHE TACYADEKPY
LYGVKDNGIS TEKSAATGQD PIEAWEEHIQ ELAKWQPHLF FKS
//