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Database: UniProt
Entry: A0A162PUB4_9PEZI
LinkDB: A0A162PUB4_9PEZI
Original site: A0A162PUB4_9PEZI 
ID   A0A162PUB4_9PEZI        Unreviewed;       742 AA.
AC   A0A162PUB4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase family m28 {ECO:0000313|EMBL:KZL87583.1};
GN   ORFNames=CI238_01468 {ECO:0000313|EMBL:KZL87583.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL87583.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL87583.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL87583.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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:KZL87583.1}.
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DR   EMBL; LFIW01000219; KZL87583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162PUB4; -.
DR   STRING; 1573173.A0A162PUB4; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; 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; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT   DOMAIN          195..259
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          383..554
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          628..741
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
SQ   SEQUENCE   742 AA;  81414 MW;  6BEB0FC77746745C CRC64;
     MTVEKVWKTS RDWTQRCHST PSGISDSFNM RRTLLAVVIA ATGIYACQRD WDALNRRINR
     HSHHDHGHKK RDLAVEYPPS LTEYETILVN SFDSKSLDEW SHYYTSGDHL GGHNRTQAEW
     TQQKWIDAGW DASIEEYWIW YTAPLETTLR LNRPDGSVHD VSLIEDMLEE DPTTSYPNRI
     PAYHAMSGSG NISAEYVYVG RGQRADFQAL KDAGIELEGK IALSMYGGIY RGTKVKNAQD
     NGMIGAVLFT DPLDDGEITV ANGYLAYPDG PARNPSMIQR GSVRFSSLYS GDPSTVGYAS
     EKDGPRNDVT PYNPTIPSVP ISMKDAAPLL AALDGSGLSA EQVNRSSWVG ALPNITYSSG
     PATGATLDMV HFMNQTIAPS WDVIGIINGT HSDEVLVIGN HRDAWVIGGA ADPNSGSAVL
     IELAKAFGKL VEKGWKPRRT IILGSWDAEE FGLQGSTEWV ESHLPWLVTN AVAYLNLDVA
     VSGPRTALSG SGEIQTVAIE MMKKVLFPEG WGVGPTLYDM WFNTTEGEIP PLGSGSDYAA
     FYHNGISAFS CGTARLTRIR HYDSYNWMAK FGDPGFKIHR VMGQWLTLIA YHIADDVIIP
     WDLPNAGRVL RTYYEDLNQT LTEDYSSLDL SPIDSAISEF EAAAERIATV AKQARAFNDT
     VLIDVVNGKY RDFSRGFASA GGLPGRPTFH NVISAPGLDN GYGADVFPAV QDSLSSGSEE
     QAQEWVDKSA SAVSRAADIL RI
//
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