ID A0A317XET7_9BASI Unreviewed; 920 AA.
AC A0A317XET7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Zn-dependent exopeptidase {ECO:0000313|EMBL:PWY96855.1};
GN ORFNames=BCV70DRAFT_203380 {ECO:0000313|EMBL:PWY96855.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY96855.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWY96855.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY96855.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KZ819251; PWY96855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XET7; -.
DR STRING; 1882483.A0A317XET7; -.
DR InParanoid; A0A317XET7; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000246740}.
FT DOMAIN 310..386
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 498..681
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 838..916
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 399..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 101514 MW; FEB04A37DC8D6292 CRC64;
MAPLPPLFYE AFDVDSRQTR YHDDYESDAK VPLMIDEKID AEAQIPVDTT ATPAQVHAWP
RLGIWIRRIA IVAWICIFYS VLSDTEPQRE PHHHHHHHDG SSSIAHWLRP FRSPCPHAQA
VRGYRNSLEA TQLLSSPAEV AATFGKDADK PANPEQRWKQ WLAKLESDFL AVPSAVGARD
ALQRYTNVSH YAGTETDYNS ALQILEEWGQ LVGAPLTDNL KELVFDAGSA ESQAYLTGAG
DKTGVRAWTD TYSVYLNQPI NSSLTLAKPD AEDAPYWTAK LAEDVLEKDP TSGRGVPLFH
GYSASGAASG QIVFAGMGRK QDFADLAAKG IDVKGKIVLV DYGGNFRGLK VRAAQEAGAV
AVIIYTDTIE DGEITEANGY AAYPDGPARN PSAVQRGSVQ GLSFYPGDPG TPGKPSYRNA
TRIAPEEADS LPKIPSLPLS YSEAKVLFEA LKGKGVRAQD VNDRLAGAID GVEYWTGPSD
DIVHLENFVD MKVRDIWNTY AVLPGHVKDE VVILGNHRDA WTFGAADPNS GTAAFHEAIK
GLGKLYKAGW RPMRTIVFAS WDAEEYGLVG STEFGEDYAE WIRKHVVAYH NVDVSVSGSQ
ILSNASPSLA RLVQDAAARV DDPNAPAGSG KKVQVNAFNP LGSGSDYTVF LQHLGIASTD
LGYKRAAKDP IYMYHSNFDS FYWMDTFGDP GFKRHEAAAK IIGLMALDSS MSIFAPLNIG
DYADELQKYF GKVQKLALKK LDVQENAPWL RELQRSIHDF RRSAHRLEHH QRHLTHKLVH
LAEKMARRHH PHGHGHGHGD GDHPHHGGEG EESQAHRLFK HPHHDHDEKL RRELWKLLGQ
IRAVNSKLQN VEKGFISPEG LEGRSWYKHL VTAPGRWLGY GATTFPGLTE AITLDNGDGL
EKEAARLTKH IHAVARQVIS
//