ID   A0A2C5ZM33_9HYPO        Unreviewed;       933 AA.
AC   A0A2C5ZM33;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Transferrin receptor-like dimerisation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDD80_6419 {ECO:0000313|EMBL:PHH80860.1};
OS   Ophiocordyceps camponoti-rufipedis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH80860.1, ECO:0000313|Proteomes:UP000226431};
RN   [1] {ECO:0000313|EMBL:PHH80860.1, ECO:0000313|Proteomes:UP000226431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Map16 {ECO:0000313|EMBL:PHH80860.1,
RC   ECO:0000313|Proteomes:UP000226431};
RA   De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT   "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT   behavioral manipulation genes and a possible major role for enterotoxins.";
RL   Submitted (JUN-2017) 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:PHH80860.1}.
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DR   EMBL; NJES01000007; PHH80860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C5ZM33; -.
DR   STRING; 2004952.A0A2C5ZM33; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000226431; 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; 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:UP000226431};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          350..438
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          542..732
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          803..925
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  102973 MW;  C49F216BAD749966 CRC64;
     MAPEKQPFYH PSPPSYDQAL AGSSRGASHV AYDNDDDVES LSARHASSQR LSHDDHVPSS
     PIAESQQLLP VSQPRASSSA ALIRNNGYRS PTVETDDEES LAGGFGGLGD DDDSDDDAAT
     VRREMEQMDM DEPPSTRGSS WPKMLPGFSL PSWTWPWPRL PELSRLRQRM AAAFDNDQGQ
     DEDAPRRRWP FNLDEEDKRR LCQVCIRFVV VLVVLTFVVL YITTTMDVRY RRFDPQDLRQ
     HVMTNVEPMR LRASVMHFSN YAHIAGTEGD YATAMDVESM FSRAGLDRIE VDEYRVYVNY
     PRKDGRAVQI MNEAGSEPVW TAKLDEDEVG GETAGRQTYA FHGLSKSGDV RGPLLYANYG
     TRDDFAHIRD RGIDTRGAIA LVRHRRSSVA PSDAGMQVKA AELAGFAGCL IYTDPADDGF
     LKGDVAPHGR WMPTDAVRRD SVGLRGWMPG DVLTPGWESE IKVPRMKVNE TTGLVGIPSL
     PLAWRDAKEL LRRLNGHGER VPAGWAGGVP DLSGGWWTGN ETSPVVRLRN EQDEQQQQPI
     WNVYGKIVGQ EQAERAVLVG NHRDSWAFGA GDPHAGTAVM IELARILGGL LARGWRPLRT
     IEFMSWDGAA YNLMGSTEFV EKRTDELREA AYAYVNLDGA VSGTKLRAAG SPALQRPLER
     AMNHVLDSRA NATLAELWRS KGGRLRGLGA GGDYAALQHT AGTSSLDLAF VIDDDDSKGV
     PVAHSSYDRL SLIEDVVDPG FAYHVLLAQL VGVLLLDLAD RPVVPFGMKV YADALKEAVS
     DLDGWIKVRM GDDKKAEREQ AVRELADAAA LVGQNAQIFD GWELEWDRNM LETGGRETLE
     LSARRFLYND RKAAFETALL DLELGGGIPN RTQFKHVVYG PQLWAPSRAD VFPAVRDTVE
     AGDWPAARRA VAKAAVVLRK AASVLTMDDG QET
//