ID A7F2F3_SCLS1 Unreviewed; 807 AA.
AC A7F2F3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Glutamate carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_12100 {ECO:0000313|EMBL:EDN95895.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN95895.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476639; EDN95895.1; -; Genomic_DNA.
DR RefSeq; XP_001587071.1; XM_001587021.1.
DR AlphaFoldDB; A7F2F3; -.
DR STRING; 665079.A7F2F3; -.
DR EnsemblFungi; EDN95895; EDN95895; SS1G_12100.
DR GeneID; 5483102; -.
DR KEGG; ssl:SS1G_12100; -.
DR VEuPathDB; FungiDB:sscle_05g040820; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR InParanoid; A7F2F3; -.
DR OMA; LWNVIGT; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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: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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..282
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 399..590
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 680..806
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 267..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 89683 MW; 22ED213C72954507 CRC64;
MGRLIDEKAM ESNERTPLFA TVIAASPRQR YQHNTIRRFF TIAATSCLIV AVYLFLLPLS
FIPRHHSHWH HDKPYQEPSA SITYEELQQI LLDTPKAEKA REWSKYYTSG PHVAGTNKSQ
VLWTQERWQE FGIESEVISY DVYLNYPRGH RLALYEKKNA KGSDVQELKV KFEASLEEDV
LEEDDTSGLD SRIPTFHGYS AYGNVTAPYV YVNYGTYGDF EDLIRLNVSL EGKIAIARYG
GIFRGLKIKR AQELGMVGAV LFTDPGDDGA NTEENGVTTY PEGPARNPSS VQRGSAQFLS
VAPGDPTTIG YPSKPGAPRQ PVDGKIPSIP SLPISYVDAL PILKALNGIG PGPQDLNKWW
DRNLGLAYKG VEYNIGPSPD NLVLNLVNDV EYVTTPIWNL IGIINGTLPD EVIVIGNHHD
AWIVGGAGDP NSGSAALNEV VRSFGVAVSK GWKPLRTIVF ASWDGEEYGL VGSTEWVEEY
LPWLNKANVA YINCDVGTSG PTFGASASPL HNKALYEVLS LVQSPNQTVP GQTVGDVWDG
SIHTMGSGSD FTAFQDFAGV PSIDLGFGPD VNHEANGGAV FHYHSNYDSF YWMDTYGDPG
FHYHEAMSKI WALYTAKLAE TPIISFNATD YADALQGYIS KTESKLDSIM IGSSSEAEDE
EARFRPSNIE TKGDINNLKL SFKDLHHRAT ALKHAAIRHD SSAEILAKQA GQDIPWWKWV
SKVKLYYKIR TVNEKYKYLE RKFLYPEGLD GRSWFKHVVY APGLWTGYAG AVFPGLVESI
DAQDYENAEK WIRIISECLE NAAEWLA
//
