ID A0A0P7B826_9HYPO Unreviewed; 557 AA.
AC A0A0P7B826;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN ORFNames=AK830_g8450 {ECO:0000313|EMBL:KPM38106.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM38106.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM38106.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM38106.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC organization and biogenesis. {ECO:0000256|ARBA:ARBA00025210}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM38106.1}.
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DR EMBL; LKCW01000144; KPM38106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B826; -.
DR STRING; 78410.A0A0P7B826; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF147; METALLOCARBOXYPEPTIDASE ECM14-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KPM38106.1};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000313|EMBL:KPM38106.1};
KW Protease {ECO:0000313|EMBL:KPM38106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Signal {ECO:0000256|SAM:SignalP}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..557
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006135488"
FT DOMAIN 248..270
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT REGION 521..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 62387 MW; E679FFBFDFB7DBAF CRC64;
MKLSVARIAA SSLLLLNAVD AAGIDAQRNI ANNGFHSAPA DSNNNARLFP FLTKLRDSAV
EFVFGRHPTK AAAQPPVLNQ LRAQYANQLV LRFNVTTADE EGALADAVAR LFLDVWAFTT
EFVDVRLHTD EVAPLLSLLP RSLRAAQSTL ILDLAAAVYQ SLPADNDPHR PDPQNDAPVL
VAPSSLGDNL FFQDYQPLPV VVRWMRLLEA MFPTYVNYIT IGKSYEGRDI PALRVGVSDT
DPMAPPRKTI VVMGGSHARE WISTSTVNYL AWSFITSFGK ERMITKLLDK FDIIFIPIAN
PDGFEYTWHI DRLWRKTRQQ TNLQFCRGLD LDRAFGFEWD GSRVQRDPCS ESYGGEKPFQ
AVEAVQIADW ARNQTWNNVR FVGLVDLHSY SQQILFPYSY TCSIDPPNLE NLEELAAGIA
KSIRLSNGES YTVASACEGA VSVRESGDER VWPRVESGGG SAVDWFYHEM RAHFSYQIKL
RDTGSYGFLL PKEHIVPTGE EIFNAMKYYG DYLLGNNGIE KFPEKDNGAH TSEDPPSSGN
DGEGHSTQEL RRRKLRR
//