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Database: UniProt
Entry: A0A0P7B826_9HYPO
LinkDB: A0A0P7B826_9HYPO
Original site: A0A0P7B826_9HYPO 
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
//
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