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Database: UniProt
Entry: L2FB14_COLFN
LinkDB: L2FB14_COLFN
Original site: L2FB14_COLFN 
ID   L2FB14_COLFN            Unreviewed;       730 AA.
AC   L2FB14;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Glutamate carboxypeptidase 2 {ECO:0000313|EMBL:ELA23256.1};
GN   ORFNames=CGGC5_14980 {ECO:0000313|EMBL:ELA23256.1};
OS   Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS   (Colletotrichum gloeosporioides (strain Nara gc5)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA23256.1};
RN   [1] {ECO:0000313|EMBL:ELA23256.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA23256.1};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   fructicola.";
RL   Submitted (AUG-2012) 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; KB021423; ELA23256.1; -; Genomic_DNA.
DR   RefSeq; XP_007287691.1; XM_007287629.1.
DR   AlphaFoldDB; L2FB14; -.
DR   STRING; 1213859.L2FB14; -.
DR   EnsemblFungi; ELA23256; ELA23256; CGGC5_14980.
DR   HOGENOM; CLU_005688_2_0_1; -.
DR   OrthoDB; 67337at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; 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; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   PANTHER; PTHR10404:SF46; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 70; 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:ELA23256.1};
KW   Hydrolase {ECO:0000313|EMBL:ELA23256.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:ELA23256.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          192..273
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          363..502
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          605..728
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          257..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  80470 MW;  DCFACA626BFB33E9 CRC64;
     MANERTPLIT NVYVGAPRPR YQNHVLRRFC TIALSSILIF WSVFFFVALF APITHEEVQK
     ILFEVPSSEK AEEWSRYYTA GPHLAGQNYS QASNVIPLAS KQHLTARQAL WTKEKWESWG
     IQSDIVAYDV YINYPVDHSL SLLSKSKDEE ESAWKVEFKA ALEEDVLEED PSSGLPNRVP
     TFHGYSASGN VTGSFVFVNY GTYQDYEDLV KANVSLEGKI AIAKYGGIFR GLKVKRAQEL
     GMIGALLYSD PGDDGKRGSA QFLSVRPGDP STPGYPSKPG APRAPVDDAT PSIPSIPISY
     ADAIPILKAL NGHGPSIKDF NKYWNRNLGL AYKGVEYNIG PTPDNVVLNL YNEQNYTTTP
     LWNVIGIVNG TIPNEVIVVG NHRDAWIAGG AGDPNSGSSV LNEVIRGVGV AVASGWKPTR
     TIVFASWDGE EYSLIGSTEW VEEYLPWLSA ASVAYVNVDV GVRGPHFSTS AAPLLHKVLR
     EITHIVPSPN QTVPGQTVGD NDEAVDQYHS NYDSFHWMEK FGDPGFVYHR TMAQILGLVV
     AELSNVPVIR FNATDYADAL SGYVDQVEAK LAAAEPVTDA VFRQRASVAV ADADAQGSQS
     QFRASLQVLR TSIAAFREKA WNLDETAAWV DWELKEDIPW WNIIRKIKLG LAFVWVNKSY
     KGIERNFLYP GGLDGRSWFK HVVFAPGLWT GYAGAVYPGL QESIDAKDYI NAVKWSGIIN
     ECVASATKGI
//
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