ID Q4WXT7_ASPFU Unreviewed; 907 AA.
AC Q4WXT7;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Glutamate carboxypeptidase Tre2, putative {ECO:0000313|EMBL:EAL92516.1};
GN ORFNames=AFUA_3G10650 {ECO:0000313|EMBL:EAL92516.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL92516.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL92516.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL92516.1}.
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DR EMBL; AAHF01000002; EAL92516.1; -; Genomic_DNA.
DR RefSeq; XP_754554.1; XM_749461.1.
DR AlphaFoldDB; Q4WXT7; -.
DR STRING; 330879.Q4WXT7; -.
DR EnsemblFungi; EAL92516; EAL92516; AFUA_3G10650.
DR GeneID; 3512340; -.
DR KEGG; afm:AFUA_3G10650; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_1_0_1; -.
DR InParanoid; Q4WXT7; -.
DR OMA; YPRKDGR; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
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 Carboxypeptidase {ECO:0000313|EMBL:EAL92516.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:EAL92516.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EAL92516.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 168..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 311..397
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 500..683
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 760..904
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..113
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 907 AA; 101190 MW; 7AC36A334759B706 CRC64;
MGNDKKFEYE SLPIPSYEEA ISSRPSSSRS HLGPDEASDD AERQGLLHNA DNTSGPGGPR
SRPHGYQPPT VESVRNSLDD LASSGTDSAR GSLEELQREL AQMDVEEAGV QSSSRRSRLG
QHFSKRFNSL SRTLSAIQFP FRRFLPNFRF TINLDGARPR FQDHSCIIML RVFGLLLVVA
LVYVFFFSNL FNLNSRFMMG QSYSAASVQN FLQGHINETN IADNLRKVTK FPHMAGTEGS
FALAEWIEQE FKNAGLDEIE MEEFQVYLNY PNEGGRRVAI VDPPGMAWEA ALEEKNEQTM
VFHGHSKSGN VTGHLVYANY GSREDFQLLA DQGIDMKGAI ALVRYYGSET DRALKVKLAE
MAGAAGCIIY SDPHEDGFRR GPAFPDGRFM PDDGVQRGAV SLMSWVVGDV LSPGFASTPQ
EKKRLSIEES PGLPGIPSIP IAWRDAQRLL QVLKGHGTKV PKEWVGGVPE VQEWWTGDGG
SPKVNLMNIL DEVERQPIYN VVGRIIGLEQ PEKKVIVGNH RDSWCLGSAD PGSGTAVFLE
LVRVFGELRT FGWRPLRTIE FVSWDAEEYN MIGSTEHVEK AIEALRENAF AYLNVDVGVT
GNNFDASGSP LFQRIVMQIL GRIADPITNE TLKDIWERAQ KKFSPLGSGS DYVAFQDIAG
TSSVDFGFTG ERFPYHSCYE NYDWMTKFGD PGFQYHKALG QFWALLLIDL ADNPILQFDL
QVYADHVHTY VTDLVAYAKS KNVPVAPQLL EDRAVGEASV SFQPLFDAAS KFKSDAEEFD
QWAQLWHDTV WGAGGFENNV MAIQRLSHNS RLASFDTQLL DLDHDGGVST LPSHITSVPD
TDSFRQIPNR TQFKHVIFGP QLWSGYDAAV FPAIRDSIDS GNWTLTQEWI DRVAKIIHRA
SNSLVHN
//
