GenomeNet

Database: UniProt
Entry: A0A1Y2W9Y0_9PEZI
LinkDB: A0A1Y2W9Y0_9PEZI
Original site: A0A1Y2W9Y0_9PEZI 
ID   A0A1Y2W9Y0_9PEZI        Unreviewed;       894 AA.
AC   A0A1Y2W9Y0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTB06573.1};
GN   ORFNames=M426DRAFT_318964 {ECO:0000313|EMBL:OTB06573.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB06573.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB06573.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB06573.1,
RC   ECO:0000313|Proteomes:UP000242955};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ111536; OTB06573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2W9Y0; -.
DR   STRING; 1001833.A0A1Y2W9Y0; -.
DR   InParanoid; A0A1Y2W9Y0; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000242955; 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:SF71; CARBOXYPEPTIDASE TRE2, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10650)-RELATED; 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:UP000242955};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        176..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          333..421
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          520..705
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          768..892
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  100368 MW;  881B3346AB2A570F CRC64;
     MPSEKSQYIP PPPIPSYDEA TRGNPSSSQP DWPPPRSPVD TRPDHETEAQ SLLSSRPRPD
     PSRRAPNGYQ QPYVESDDEG SQWTLEDDDD SDDGEGARVR REMQELEVED PLDDSSSRSS
     SSSWRKRIAS SLPQWKWRWR LPRLTVRLPR QNDTSNDEET ESSETRRFRW PTVNSAAAVL
     LVGRLLAIFL ILGFLYLLFM SDLFTNMTRR IGGHMFDPEA VRQYVQGEIN SETMRNTLKH
     FTSYAHIAGT EGDYALAMDV RNDFMKYGLE DVSVDEYYVY LNYPKAGGRT VQIISEDGKE
     AKWTAALEEE DVGEEMTGRQ TFVFHGHSKS GNVRGPLIYA NYGSREDFKR LSDKGIDTKG
     AIALVRYYGT QGDRALKVKA AELAGFAGCI IYSDPADDGF LKGEPAPNGR YMPADGVQRG
     AVSLMSWVVG DVLTPGWESK KGLPRMDKDK TDGLVKIPSI PIAWRDAQVL LQHIQGFGDP
     CPDEWHGGVP EVEWWSGNSS SPIVRLKNEQ DEEDKQEIWN VYAKIAGVEQ SEKSIIIGNH
     RDAWAFGATD PNSGTAVMLE VARIFGDLLS RGWRPLRTIE FMSWDAEEYN LIGSTEFVEK
     NLESLQKNAF AYINLDTAVS GQEFHAAASP VYRKLLYKVL DRVIDPNANA TLRALWDDRN
     AELEGLGAGS DYVAFQDIAG TSSIDIRFDG AAHPYHSSYD NFDWMDRVGD PGFIYHNLLG
     QVLGLLILEL ADRPIMPFDM GNYALALGRY LGNLWQWGEE KGTNKRYDLE PIKNAIGEVE
     KAVVDFEKWE GSWEATVVAS NGWEPVGLGQ RRGDYNSRMA NFETGLLDLE LGGGIPNRTQ
     FKHVVFGPQL WSGYDEAYFP AIRDAIEVEN WPLAQKIINK TADIISRAAK ALVD
//
DBGET integrated database retrieval system