ID A0A1Y2UTN4_9PEZI Unreviewed; 802 AA.
AC A0A1Y2UTN4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase M28 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M434DRAFT_399292 {ECO:0000313|EMBL:OTA87888.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA87888.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA87888.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA87888.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KZ112552; OTA87888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2UTN4; -.
DR STRING; 1001938.A0A1Y2UTN4; -.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000194361};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..283
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 399..585
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 680..801
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 802 AA; 89158 MW; 7041C0D8FFF2A36E CRC64;
MKPSESNLGR NDKMANEHTP LITTVTVGTV RRRYPHQTVR RFCTIALGSS LIALFITFLV
TVVFAPSHSS HRGFPGHGKT ISFDELKDIL INTPSSDRAA EWSKYYTSGA HLAGKNLSQA
EWTRDRWNEW GIRSDIVAYE TYINYPVDHR LALLEKSKSD SPDVGVWRVA FEATLEEDVL
EEDPTTQLEE SIPTFHGYSA SGNVTGSFVY VNYGTYWDFE DLIKANVSLE GKIAVARYGG
IFRGLKVKRA QELGMIGTVL FTDPGDDGKI TEENGYDTYP NGPARHPSSV QRGSVQFISI
APGDPTTPGY PSKPGVPRAS VNGSIPSIPS LPISYAEALP ILKALNGLGP RAKDFGEYWT
INNGLGYKGV EYNVGPSPDN VVLNLYNEQE YTITPQWDVI GIINGTISDE VIVVGNHRDA
WIAGGAGDPN SGSAVINEVI RSFGQALEQG WKPLRTIVFA SWDGEEYGLI GSTEWVEEYL
PWLSATNVAY LNVDVGVRSP VFEAYAAPLL HKLLYEVTAL VQSPNQTVKG QTVRDLWDGR
IGTMGSGSDF TAFQDFAGIP SIDMGFGGGN EDSPIYHYHS NYDSFHWMSE FGDPGFAYHR
TMAQILSLAA AKLAETPLIP LNATDYAVAL KEYVEKVEAR LESFQPEHST EKDMFEFRAR
TVRSGVQGDP EQFKEILGHL YYIVGEFKKA AIELDAKSEE LAKKANEHIP WWKWISKLKL
FHEIRAINTK YKKLERSFLH PLGLDGRPWF KHVVFAPGIW TGYAGAVFPG IVESIDNNDY
VNAIKWVWII NDRIAAAIET IR
//