ID A0A423XBW9_9PEZI Unreviewed; 956 AA.
AC A0A423XBW9;
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=Bacterial surface antigen (D15) domain-containing protein {ECO:0000259|Pfam:PF01103};
GN ORFNames=VPNG_04411 {ECO:0000313|EMBL:ROW13495.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW13495.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW13495.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW13495.1,
RC ECO:0000313|Proteomes:UP000285146};
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR602640-2};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC 2};
CC -!- PTM: Glycosylated. {ECO:0000256|PIRSR:PIRSR602640-4}.
CC -!- SIMILARITY: Belongs to the paraoxonase family.
CC {ECO:0000256|ARBA:ARBA00008595}.
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:ROW13495.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKEB01000019; ROW13495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423XBW9; -.
DR STRING; 1230097.A0A423XBW9; -.
DR InParanoid; A0A423XBW9; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004064; F:arylesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.160.50; membrane protein fhac: a member of the omp85/tpsb transporter family; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR PANTHER; PTHR11799; PARAOXONASE; 1.
DR PANTHER; PTHR11799:SF12; PARAOXONASE-RELATED; 1.
DR Pfam; PF01731; Arylesterase; 1.
DR Pfam; PF01103; Omp85; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR602640-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146}.
FT DOMAIN 174..526
FT /note="Bacterial surface antigen (D15)"
FT /evidence="ECO:0000259|Pfam:PF01103"
FT ACT_SITE 658
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 660
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 736
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 737
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 844
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 845
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
SQ SEQUENCE 956 AA; 102492 MW; B48CC9A2EAC0B07C CRC64;
MASNQSSDGI SAIEALKKLE TDAAILRQEA HNMEEAELLQ NQQALQRRLE LLSDHLQRPA
TINSIEVHGA RNTRKGFLDP IFAPLVGNSR NAGTTLGEIL AGVQEATSKL DRFEIFRPEP
TVYLNDARDS SPHAASTDID VSIRVAERSR FLLKGGTDLG NSEGSGYINL LWRNVFGGAE
QLSVNTSAGT RTRSAYNAAF SAPVDGNPDF RVSVEGVSSD TQKPWASHDE VVRGGSLKAA
WLSQQGDLHN LAYSGAWRQI TGLSATASPT VRADAGDSLK SSLIYTFTRD RRDNPMLPQR
GYLFKTVTEL AGVGPLRGDV AFSKSEVEVG GALPVALPGI SSSRTGISIG GGLRFGLLYP
LALGWSPRGE AKPSLINDRF QLGGPTDVRG FKLGGLGPRD GGDSVGGDVF AAGSVNVLLP
LPRAGADSPL RLQLFANGGR LVALDNEDKT QEKPGKGLAL RPSAVSNGIT RALGELGNGL
PSLAAGFGLV YAHPVARFEL NFSLPLVVRR GEQMRKGLSV GVGINFFESK SMASVGIVVA
ALAGLAAYVY GPATHGVLTK FGAFRELQSS PLAHPGDLVS VKDTTHCEDL HYYPPAHTLF
TACEDASATR FGWFPPLVFY DDPYVAWNSK GSIHTIDPET KESKRLDFEK FDGPFITHGI
DVIGDPETPE GEAVYIFAVN HVPNEAVYPR DPGAPKTDPG TAPKVASRIE VFHHVIGSAS
VKYIRTIAHP SIKTPNDIYA ISPYEVYVTN DHYYLEGYLR VLEELWPTTK WSNVVHATVS
EDGSVQATVA LDKLHNPNGL GHGRTKDEIL VGSAVGGNIW TGKLGSADKT IAVVERIDVD
STIDNPSYFS DPYPEVGGDA SGFILSGLTR AIDLGKVGQD PLGKEGVLVW YVTPNKNTTG
TWDRKLLWQD DGSNIRNAAT AVLVGIDPKK EDGKKRAWLF VTGFSSENAV AVKVDL
//
