ID M7SIB8_EUTLA Unreviewed; 740 AA.
AC M7SIB8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative glutamate carboxypeptidase protein {ECO:0000313|EMBL:EMR66064.1};
GN ORFNames=UCREL1_6954 {ECO:0000313|EMBL:EMR66064.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR66064.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KB706718; EMR66064.1; -; Genomic_DNA.
DR RefSeq; XP_007794846.1; XM_007796655.1.
DR AlphaFoldDB; M7SIB8; -.
DR KEGG; ela:UCREL1_6954; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_2_0_1; -.
DR OMA; TEWMEEY; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
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; 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; 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:EMR66064.1};
KW Hydrolase {ECO:0000313|EMBL:EMR66064.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EMR66064.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT DOMAIN 378..563
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 627..739
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 263..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 79922 MW; 86CFD6398245F14B CRC64;
MHNVTSSTKY STDIVSTIWQ VKITATSQLN VTATVIPRIS PHVDPGLWSK VGTVKRQDSR
QIPLKLEDSP DGPGLSLNSD ERTLVESVSN TTLSGWSYYY THGDHVAGRN RTMAQWTADR
FAESGINSSV VSYNVYLNYP VNKSLTLTWS NGTIYEPSLE EDVLSEDDTS SYPNRIPTFH
GYSASGSASA EYVYVGRGQQ VDFERLVELG VPLEGKIAIA KYGGPFRGLK VKNSQDYGLV
GTVIFTDPGD DGNVTEANGY AAYPDGPARN PSSVQRGSVQ FLSTYPGDPT TPGYPSKPGS
PRADKSPVVP RIPSIPISYQ DAIPILAALD GYGTAGDVVN RTGWVGALNV SYSTGPAPGA
TLSLSNLMDE QYTDIWDTIG VINGTNTNET IIIGNHRDAW IVGGAADPNS GSAVLVELSK
AFGKLLAQGW KPKRNIVLAS WDAEEYGLVG STEWVEEYIP WLTDTAVSYL NIDVGTAGPH
PDISATPELH TIAIDTMKKI LWRDTGRTMY DVWYDDFEGE VGVLGSGSDY TAFVHNGIGS
IDLGSGGGAT DPVYHYHSNF DSYHWMATYG DPGFLSHKSM AQYLSLLAYN IAAPDLIPFD
LPNYATQLET YYESLTSTIS SASADLDISA LRGAIDEFAG RTAEVKAQEQ QALSTDDSGL
LTLVNQKYRD FQRGFVSQGG LPNRTFYKHL IFAPGLDTGY APTTFPGITE AVESGNLTLA
TEFVKKTADA ITKAGDILKA
//