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Database: UniProt
Entry: A0A094HGU8_9PEZI
LinkDB: A0A094HGU8_9PEZI
Original site: A0A094HGU8_9PEZI 
ID   A0A094HGU8_9PEZI        Unreviewed;       808 AA.
AC   A0A094HGU8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Peptidase M28 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V501_03155 {ECO:0000313|EMBL:KFZ14610.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ14610.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ14610.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFZ14610.1}.
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DR   EMBL; JPKD01001093; KFZ14610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HGU8; -.
DR   STRING; 1420914.A0A094HGU8; -.
DR   HOGENOM; CLU_005688_2_0_1; -.
DR   Proteomes; UP000029315; 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:UP000029315};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..292
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          406..593
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          681..805
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   808 AA;  88827 MW;  E9E2F31EE4B01366 CRC64;
     MHLLPSPSRQ GHLPAAMAPD DRTPLLGASS TAQPARLPQQ QSSAAVRRRF AYIAAGSLAI
     AFVILVLIPA AFIPHLLDDL VPSRGKFQYA DLENLLLNSP STEKLSEWSK YYTSGPHLAG
     TNLSQAVWTQ ERWKEFGIED SSVVPYEVYL NYPLGHRLAL LEKPSKGHSK DDEATWKVKF
     EASLEEDVLE EDPTTGASNR IPTFHGYSAN GNVTARYVYV NYGTYHDFED LIKANVSLEG
     NIAIARYGHV FRGLKIKRAQ ELGMVGAVLF TDPGDDGTPL HDMSENYPDG PGRNPSSVQR
     GSAQFLSMGP GDPTTPGYPS KPGVPRSPTD DNIPRIPSIP ISYTDAIPIL KALNGHGPVP
     KDLNKYWNVN LGLVTRGVHY NAGPSPEGLV LKLVNEQDYK ITPIWNVIGI INGTLSDEVV
     VVGNHRDAWI VGGAGDPNSG SAAMMEVIRG FGQALSKGWK PLRTIVFASW DGEEYGLVGS
     TEWVEEYIPW LSEANVAYVN IDVGCSGPKF VAAASPLLNN LIYEVTGRVQ SPNQTVEGQT
     VRDVWGGHIS TMGSGSDFTA FQDFAGISSI DIGFTASEES AVYQYHSNYD SYHWMETYGD
     PGWHYHATIS KVLGLFVAKL ADSPLVPFRT TDYGTALISY VQQIQDLVDN GPARSSTIRF
     RPTPEASTDS ASRHKHLGRG LKHMQGSAHR FLEAARVFDE HVDKLRERAE HGYGWLRWCA
     RLKLYLAVRK ANFAMKLLDR KFLHAPGLTG RSWFKHVIFA PGLWTGYAGA VFPSLAEAID
     NEDGMGAIGW MQIINDKIIE ATRSLELY
//
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