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
//