ECM14_ARTGP
ID ECM14_ARTGP Reviewed; 593 AA.
AC E4UPZ6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=MGYG_02142;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC organization and biogenesis. {ECO:0000250|UniProtKB:P38836}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P38836}. Secreted
CC {ECO:0000250|UniProtKB:P38836}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue in position 512 essential for
CC carbopeptidase activity. The mature form lacks catalytic activity
CC towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}.
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DR EMBL; DS989823; EFQ99130.1; -; Genomic_DNA.
DR RefSeq; XP_003174613.1; XM_003174565.1.
DR AlphaFoldDB; E4UPZ6; -.
DR SMR; E4UPZ6; -.
DR STRING; 63402.XP_003174613.1; -.
DR EnsemblFungi; EFQ99130; EFQ99130; MGYG_02142.
DR GeneID; 10029910; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR InParanoid; E4UPZ6; -.
DR OMA; SACEGNV; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Metal-binding; Reference proteome; Secreted; Signal; Vacuole; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..184
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453233"
FT CHAIN 185..593
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000411174"
FT REGION 180..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 360..361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 418..419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 354..377
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 593 AA; 66239 MW; A1676CB5938888D9 CRC64;
MHFSVRLSLL LTLASSLPLV SAIPQHEDQA YTFPSPGRSA TANTDPVLEV GRETQRTPSA
WTRLRDSLVE SVWGLPQRKE GGEWRTRNQV TTASRAPATL QARYGEDVVL RFTIKTQEEV
KALVEASNIL FLDVWGSHDD WVDIRLSRDV IPSLLGLLPP SLQSSHVPLI RDLAQTIYES
YPKTNPSSPS QQGPTTRRFS PSASTSKTKP QETKNIFFQD YQPLSVLLPW MRLLVSMFSS
HATLISVGTT AEGRDIPALR VGVHPTNNAQ QAPRRRTIVI SGGAHAREWI SVSTVSYIAY
SFITGYGKSR SITKLLEQFD YVFIPTVNPD GYAYTFSTDR LWRKNRQQTS LSFCPGIDLD
HSWGYEWDGN ATRSNPCSEN YAGDQPFEAI EAREIATWAR KEVTVNNVQF VAFVDLHSYS
QQILYPYGHS CAHLPANLEN LEELGAGLAK AIRKTSRENY DVKAACRGIV ASSMGDKDAD
EAVTSSALES TAGSALDWFY HDMDVRFSYQ IKLRDRGSYG FLLPREQIVP TGKEIYRAMV
AMGKFLVSPH ILTGDLNGPH AAEETQNYDD DFEEDEAEED SDVFRAQGDD MSS
