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
//