ID A0A1L9RX38_ASPWE Unreviewed; 767 AA.
AC A0A1L9RX38;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Peptidase M28 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPWEDRAFT_37285 {ECO:0000313|EMBL:OJJ39496.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ39496.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KV878210; OJJ39496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9RX38; -.
DR STRING; 1073089.A0A1L9RX38; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_37285; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000184383; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR PANTHER; PTHR10404:SF46; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 70; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..272
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 389..579
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 640..767
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 767 AA; 84367 MW; F341957B0D5F98A2 CRC64;
MAPSESTPLL YVQVAPQRHR YPHHTLRRFC TSILGLTLFL SLVVFLIPVA LLPRGYRTYI
PGAHSLPHAA WPHGNGLGYQ ELQALLQEIP SAAKAKEWSD YYTAGPHLAG KNLTQALWTR
QKWQEFGVQD TGLAAYDIYL NYPADHRLAL LKKTGDASPE VTFEATLEED VLKEDHTSGL
PDRVPTFHGY SASGNATAQF VYVNFGTYAD FDDLVKANVS LSGKIALVKY GRIFRGLKVK
RAQELGMVGV IMYDDPQSDG EITEENGYKP YPEGPARNPS AVQRGSVQFL SFAPGDPTTP
GYPSLPGCDR QDPSDAIPSI PSIPISYNEA LPFLKALNGH GPKASDFNQY WQGGGLAYKG
VEYNIGPSPE DVVINLYNQQ EYVTTPLWNV IGTIKGSIPD EVIILGNHRD AWIAGGSGDP
NSGSAALNEV VRSFGEALKA GWKPLRTIVF ASWDGEEYGL LGSTEWVEEN LPWLSKANVV
YLNVDVGASG THFKASASPL LNKVIYEVAG LVQSPNQTVA GQTILDVWDG KINTMGSGSD
FTAFQDFAGV PSFDLGFGRS SNDPVYHYHS NYDSADWMDR FGDPSWRHHE AIAKVWALAA
AQLSETPVLA LNATDYAHGL GDYLERIKPN AENLPSGSNF SFDDLNLAIV HLHNVAAQFD
AQAAELASHL DDDLPWYLWW KKIALYVQIR NVNSKYKGIE RELLYQPGLD GRNWFKHVVF
APGIWTGYSG STYPGLVESF DAGDVANAKK WSSIIQERIY SAAKLLE
//