ID W9IEI6_FUSOX Unreviewed; 800 AA.
AC W9IEI6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glutamate carboxypeptidase II {ECO:0000313|EMBL:EWY93052.1};
GN ORFNames=FOYG_06404 {ECO:0000313|EMBL:EWY93052.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY93052.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY93052.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; JH717842; EWY93052.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IEI6; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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 Carboxypeptidase {ECO:0000313|EMBL:EWY93052.1};
KW Hydrolase {ECO:0000313|EMBL:EWY93052.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EWY93052.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..280
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 398..583
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 673..798
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89177 MW; DF40E0D55DDFA944 CRC64;
MSRINSSHQE QEKMPDENTP LIQTVQVGPP RRRYPHQTWR RFFTLICSAI LIGGFGLFVF
QTFFIGPRHH HGHPGSWLPG KSRLSYEELE RILFDTPDPK KAEEWSRYYT SGPHLAGANY
SQAEWTRDRW EEFGVKSEIV AYDAYLNYPV DSSVSILKKS KNGKDWDTTF KASLEEDVID
EDPTTSLENR VPIFHGYSAS GNVTASFVYV NYGTYQDYQD LVDAKIDVKG KIAIARYGGI
FRGLKVKRAQ ELGFVGILIY SDPGDDGERT EENGYKPYPE GPARNPSAVQ RGSAEFLSIR
PGDPSTPGYP SKPGVPRAPV DDATPSIPSI PISYRDALPI LKALNGHGPK STHFNKYWNK
NLGLKYKGIK YNIGPTPDDV VINLYNEQKY VTTPLWDIIG VVNGTIPNEV IVVGNHRDAW
IAGGAGDPNS GSAVINEVIR GVGKAVEAGW KPLRTIVFAS WDGEEYSLIG STEWVEEYLP
WLSEANVAYV NVDVGVDGPE FTASAAPLLN QIIRDVTSAV PSPNQTIPGQ TVNDLWSGRI
ATMGSGSDFT AFQDHAGIPC IDFGFKYRGN SAVYHYHSNY DSFYWMKEYG DVGFKYHRTM
AQILGLTIAK LAGTVIIPFS ATEYADALEG YLDKVEAKLE PSKDTLTEEE IFNIRGTVSS
GKPIGNEDDF KTSLKDIRDL LGHFHLKASE LDAEAEIAKH QLEQGIPWWN IVEKIRLGYT
IVRVNRRYKL LERSFLYEGG LDGRDWFKHV VFAPGIWTGY SGAVFPGWVE SIDAKDYING
LKWSAIIGRS INSAIDGLSD
//
