GCP1_ARTBC
ID GCP1_ARTBC Reviewed; 727 AA.
AC D4B1R0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Probable glutamate carboxypeptidase ARB_02390 {ECO:0000305};
DE EC=3.4.17.21 {ECO:0000250|UniProtKB:Q04609};
DE Flags: Precursor;
GN ORFNames=ARB_02390;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-
CC acidic dipeptidase (NAALADase) activity (By similarity). Also exhibits
CC a dipeptidyl-peptidase IV type activity (By similarity).
CC {ECO:0000250|UniProtKB:Q04609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21; Evidence={ECO:0000250|UniProtKB:Q04609};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04609};
CC Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.
CC {ECO:0000250|UniProtKB:Q04609};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; ABSU01000027; EFE30692.1; -; Genomic_DNA.
DR RefSeq; XP_003011332.1; XM_003011286.1.
DR AlphaFoldDB; D4B1R0; -.
DR SMR; D4B1R0; -.
DR STRING; 663331.D4B1R0; -.
DR EnsemblFungi; EFE30692; EFE30692; ARB_02390.
DR GeneID; 9524233; -.
DR KEGG; abe:ARB_02390; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR OMA; PGDDGNM; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.40; -; 1.
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; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..727
FT /note="Probable glutamate carboxypeptidase ARB_02390"
FT /id="PRO_5003054615"
FT DOMAIN 158..296
FT /note="PA"
FT /evidence="ECO:0000255"
FT REGION 255..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..565
FT /note="NAALADase"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT ACT_SITE 414
FT /note="For NAALADase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT ACT_SITE 604
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 665
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 516..518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 530
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 675..676
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 727 AA; 79197 MW; AFCABEF21B90621D CRC64;
MIVKSLSLLA LAAATVEGCV RERDVGSVDI LSVLSKRGHG HPHLPHLSKY ESMLINSFDN
TTVDSWAYYY THGIHIAGTN QSMAQWTADK WTEFGIPSSL VSYDVYLNYP VSHSLSLTHP
DGTTWEASLV EDVLKEDDTT SYPDRIPTFH GYSASGEATA EYVYVGRGQK VDFERLIQLG
VDLKGKIAIA RYGGPFRGLK VKNAQDQGMI GCIIFTDPAD DGNVTVANGL KAYPNGPARN
PSAVQRGSVQ FLSMFPGDPT TPGYPSRPDS PRKDKSPVVP KIPSIPISQL DAQPILAALD
GHGTPGKEVN RTRWVGALNA TYATGPAPGA KLSMSNVMRD TYTPIWNSIG IINGTEQDEV
VIIGNHRDAW IIGGAGDPNS GSSIMVELAK AFGKLQKAGW KPKRTIVMCS WDAEEYGLVG
STEWVEEYLP WLKASAVAYL NIDVAVSGPV PDLSATPELH KLALESMKKV IWPYKGRQDT
TMYDVWNTAS GGEVGVLGSG SDYTAFVHNG IASLDTGAGG DGNTDPVYHY HSNYDSYHWM
ATYGDPGFHT HVAMGQFLGL LGYHLATDDI IPFDVTNYGV QMTKYLDVLK KYIAASKFPD
LDVSKIESAI CSFNVSANAV AKLQKKAEHN VHDQQLRKHL NTIYRDFGRG FVSQGGLPDR
EFYRHMLYAP GLDTGYAPTT FPGVTESLDA GNRTRAVEYI ERASNAIYVA AGILSSCHDC
NQFVAQE
