(data stored in ACNUC8465 zone)

SWISSPROT: ECM14_PENRW

ID   ECM14_PENRW             Reviewed;         522 AA.
AC   B6H233;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   RecName: Full=Putative metallocarboxypeptidase ecm14;
DE            EC=3.4.17.-;
DE   Flags: Precursor;
GN   Name=ecm14; ORFNames=Pc13g03770;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Probable carboxypeptidase that may be involved in cell
CC       wall organization and biogenesis. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
DR   EMBL; AM920428; CAP91446.1; -; Genomic_DNA.
DR   RefSeq; XP_002558814.1; XM_002558768.1.
DR   ProteinModelPortal; B6H233; -.
DR   SMR; B6H233; -.
DR   STRING; 500485.XP_002558814.1; -.
DR   EnsemblFungi; CAP91446; CAP91446; PCH_Pc13g03770.
DR   GeneID; 8313477; -.
DR   KEGG; pcs:Pc13g03770; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   eggNOG; COG2866; LUCA.
DR   HOGENOM; HOG000214206; -.
DR   KO; K08783; -.
DR   OMA; YSQQILY; -.
DR   OrthoDB; EOG092C238F; -.
DR   BioCyc; PCHR:PC13G03770-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H233.
DR   SWISS-2DPAGE; B6H233.
KW   Carboxypeptidase; Cell wall biogenesis/degradation; Complete proteome;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal; Vacuole; Zinc.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    522       Putative metallocarboxypeptidase ecm14.
FT                                /FTId=PRO_5000408934.
FT   REGION      251    254       Substrate binding. {ECO:0000250}.
FT   REGION      326    327       Substrate binding. {ECO:0000250}.
FT   REGION      384    385       Substrate binding. {ECO:0000250}.
FT   METAL       251    251       Zinc; catalytic. {ECO:0000250}.
FT   METAL       254    254       Zinc; catalytic. {ECO:0000250}.
FT   METAL       383    383       Zinc; catalytic. {ECO:0000250}.
FT   BINDING     309    309       Substrate. {ECO:0000250}.
FT   CARBOHYD    367    367       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    320    343       {ECO:0000250}.
SQ   SEQUENCE   522 AA;  58450 MW;  28FEDEC149AC189B CRC64;
     MRLFSPILVA STLIPLISAV PAGSSITPPP PLQPSYFTHS SPRPWARLRD WIIGSIWDID
     HKHRSSKHSS PPSNIHDRYG SDVVLRFHLR QPDEAEALAS ASQVLFLDIW AITSEFVDIR
     LADDMIPSLL DLLPLTLRTS YTPLMDNLAD EIYASYPSRH RSDSDFKSGL ASAELKTISN
     CDLFFQEYQP LSVITQWMRL MASMFSSHVR MTSVGVSYEG RDIPALRLGT SHNTETTSGP
     RKTILIVGGS HAREWISTST VTYVAYSLIT HYGYSPAVTR LLHEYDWVLI PTINPDGYVY
     SWESDRLWRK NRQPTGLPLC PGVDLDRAWD YEWDGESTRS NPCSENYAGA EPFEALESQR
     LAQWAQNQTA HGGAEIVGFL DLHSYSQQIL YPYSYSCSSV PPTLESLEEL ALGLAKAIRQ
     TSHESYDVTS ACEGILTQGA AAGITSGGSA LDWFYHKLHT RFSYQIKLRD RGSYGFLLPS
     EHIVPTGKEI FRALLTFGKF VWGEEASDIS LEDMTGDQIP LN
//

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