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Database: UniProt
Entry: A0A165Q2M2_9APHY
LinkDB: A0A165Q2M2_9APHY
Original site: A0A165Q2M2_9APHY 
ID   A0A165Q2M2_9APHY        Unreviewed;       516 AA.
AC   A0A165Q2M2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Bacterial surface antigen (D15) domain-containing protein {ECO:0000259|Pfam:PF01103};
GN   ORFNames=DAEQUDRAFT_711147 {ECO:0000313|EMBL:KZT68930.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT68930.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT68930.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT68930.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004374}.
CC   -!- SIMILARITY: Belongs to the SAM50/omp85 family.
CC       {ECO:0000256|ARBA:ARBA00010913}.
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DR   EMBL; KV429062; KZT68930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165Q2M2; -.
DR   STRING; 1314783.A0A165Q2M2; -.
DR   OrthoDB; 46657at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.40.160.50; membrane protein fhac: a member of the omp85/tpsb transporter family; 1.
DR   InterPro; IPR000184; Bac_surfAg_D15.
DR   InterPro; IPR039910; D15-like.
DR   PANTHER; PTHR12815:SF18; SORTING AND ASSEMBLY MACHINERY COMPONENT 50 HOMOLOG; 1.
DR   PANTHER; PTHR12815; SORTING AND ASSEMBLY MACHINERY SAMM50 PROTEIN FAMILY MEMBER; 1.
DR   Pfam; PF01103; Omp85; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          190..515
FT                   /note="Bacterial surface antigen (D15)"
FT                   /evidence="ECO:0000259|Pfam:PF01103"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  55407 MW;  CA918DE90C44FEBB CRC64;
     MADAGSTLDA PPLKPPLANT SAPRDKEPKE ADFEKLRKWQ EERIARKLRG EYESAVLHLA
     EVVNDNLNTP LRLAAIRVEG AVRTRQSFLS ALVTPFLPRP VSPSFGASSE PPSTLGDALH
     TARHLGSLLQ ETDIFQSVEA RLEGSRDFLA RPGDVDLVFR TRERGRFYLN TSTQVGNNEG
     GASATCRVRN AFGSAELFQA NLAFATTTRV AFSASLSAPL LPYLPYAPSP SPNPDLSTRG
     EISVFGHERD NTTFASSFEG VRGLRAAVRT GTPRNGTHEF AYEGVLRHIG NLAPTASISI
     REAAGPSIKS ALSHSFMRDT RDDALLGTRG SYVKLSHELA GLGGDASFYK AEGAAQLARR
     LVPGVTVSLA AKTGLLWGLD GRPAPFSDRF QLGGPMNVRM FRANGLGPQD GPDSLGGDMY
     WAAGLSVVSD IPKKPHWPVK LHGFVNLGRL DTRDKSQSLI DNMRESISKP SVGAGVGLVY
     KLDAVRVEVN FGVPLVASKS DGVRKGIQVG IGLDFL
//
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