ID A0A1X6MVM0_9APHY Unreviewed; 917 AA.
AC A0A1X6MVM0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Zn-dependent exopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=POSPLADRAFT_1070696 {ECO:0000313|EMBL:OSX60408.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX60408.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX60408.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX60408.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KZ110600; OSX60408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6MVM0; -.
DR STRING; 670580.A0A1X6MVM0; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000194127; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 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; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000194127};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..316
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 404..544
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 830..914
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 917 AA; 101745 MW; DAFC20F53C9F1C86 CRC64;
MASEKLSMSF YDKQPHPIPA PVVATAPPTA RGNRAVFWRK LVVTSLAALS LLYYVGCWFC
ALRQRIDAQE GRWIAQAFGA HPPRNLGYRR IPFGKAAEEI FLAVPNPASA IAASRQYATT
PHLAGSPGDY RTATDFLALL QTELSIEAPT PLPVFSAGTA ESRNATLSIS EGLNGPTAWI
DTYYPVMNTP LDRRVEILDE DGEVVWSADL EEQADETDPE AGKYKDAVPT FHGLSRGGEV
QGKLVYAHYG RKQDYDALVE QGVDLNGSVV ITRYGGIFRG LKVKGAQDLG AVACLIYSDP
RDDGTVTEEN GYEPYPMGPA RNPTSVQRGS TQFLSIYPGD PTTPGYPSYE NSTRSEGSNI
PSIPSLPISW ANAKVLLEEI ADGGKDRTIS LVNHVDDRVI PIWNTMGVIP GHIKDEVVVV
GNHRDAWVMG ATDPSSGTAS IHEVVRGLGA LLKEGWTPLR TIVIASWDAE EYGLIGSTEW
GEDFADWIDE HVVAYVNLDS SVGGSRFYSS SSPSLAHFMR GAAESIAHPT KPGLTLWDAT
QDRGPLYGTH GRVDEEAVRV YEEEQAQLAA AAADELGVGV LGSGSDYTVF LQRIGVASTN
NGFTSTLSDP VYHYHSVFDS QRWQELYADP GFLRHVAIAK FLGLQTLRLV DSIILPFNTT
HYAVQLGAYL DHVEQIALAA SLDVDFSDLR ESIDSLYAAS QSLDEEKFKA EHEIKRFIRR
IVRRRLIKRH LRRAWCTIKK VFGKPCAERR LNAVEGVHHQ LDEPRSNHVA PPFQKRDGRA
FKPRVGLWGG KMWEREQHAR EHAHERSGGC QVQWRARARP NFDDKLRERF RQVVKRVRTV
NKKLGSFERG FIHPDGIKDR EWYRHLGVAP GKWLGYGATT LPGLTEAITF EANATLVRYE
AERLQELIDR LAEEILP
//