ECM14_ARTOC
ID ECM14_ARTOC Reviewed; 593 AA.
AC C5FPR9;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=MCYG_04493;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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 503 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; DS995704; EEQ31674.1; -; Genomic_DNA.
DR RefSeq; XP_002846756.1; XM_002846710.1.
DR AlphaFoldDB; C5FPR9; -.
DR SMR; C5FPR9; -.
DR STRING; 63405.XP_002846756.1; -.
DR EnsemblFungi; EEQ31674; EEQ31674; MCYG_04493.
DR GeneID; 9229870; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; SACEGNV; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000002035; 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..175
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453257"
FT CHAIN 176..593
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000390758"
FT REGION 75..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 276..279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 409..410
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 345..368
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 593 AA; 65753 MW; 2D07FF4D48457ED0 CRC64;
MHVTVQLSLL LSLASSLPLV SAIPQHDGQA YTFPSTGRSA TADTDPVLEV RQGAYRPPSA
WTRLRDSIVE SVWGVPQRGK DSETKTGKQS EAASKAPATL QARYGEDVVL RFTIKTQEEM
KALVEASNIL FLDVWGTHDD GIPSLLGLLP PSLQTSHVPL IRDLAQAIYE SYPKNNPSSP
SHPGATTRRF SPSASTPESQ PHETKNIFFQ DYQPLSVLLP WMRLLVSMFS SHTTLISVGT
TAEGRDIPAL RVGVHPTNNA QQAPRRRTIV ISGGAHAREW ISVSTVSYIA YSFITGYGKS
RSITKLLEQF DYVFIPTVNP DGYVYTFSTD RLWRKNRQST SLSFCPGIDL DRSWGFEWDG
NATRSNPCSE SYAGEGPFEA IEAREIADWA RKEVTENNVH FAGFVDLHSY SQQILYPYGH
SCAHLPANLE NLEELGAGLA KAIRRSSREI YDTKAACRGI VASGAREKGT NEPVASYALE
STAGSALDWF YHDLDVRFSY QIKLRDRGSY GFLLPREHIV PTGKEIYHAV VAMGKFLVSP
HILEEEVDEP HAGEQTQDNS YDEDGDNLFR AQGGDPQVRF TRRNIGAHDD DSE
