ID A0A1E3HQI9_9TREE Unreviewed; 417 AA.
AC A0A1E3HQI9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN ORFNames=L202_04216 {ECO:0000313|EMBL:ODN78619.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN78619.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN78619.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN78619.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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 -!- 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:ODN78619.1}.
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DR EMBL; AWGJ01000006; ODN78619.1; -; Genomic_DNA.
DR EMBL; AWGJ01000006; ODN78620.1; -; Genomic_DNA.
DR RefSeq; XP_018993665.1; XM_019138229.1.
DR RefSeq; XP_018993666.1; XM_019138230.1.
DR AlphaFoldDB; A0A1E3HQI9; -.
DR GeneID; 30155525; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000094065; Unassembled WGS sequence.
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 Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF147; INACTIVE METALLOCARBOXYPEPTIDASE ECM14; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..417
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009448986"
FT DOMAIN 195..417
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 46373 MW; 67F2AC42EB728EDB CRC64;
MPSSMTNSIS LLLVVLPLLA LAAAHEPLTP LPPTDGQRPL SVPPLPAQSS SGSGGWRSSE
RYYGEQVWRI RLGGGDLARM GDILESVDDL DLDIWGTTAT TIDIRLTDRQ KDMLESALKL
ESESALESFI PDLQALIEAT APTHHDISDS GFQDPLHQDL EESSGRPEIS KKKSKPPKPD
PFNLTTLLTP FHDSYHSLAD IAKFGDRLVE TFNGEQGLEV WDFTVGTSWE GREIKGWSAR
FGNEPDNGED GDEEPRREIV IMSGQHGREW VGPSSALYFL HSTILSALYP SINPDPSLLL
RHFTVTIIPL INPDGFEYSQ HHRMWRKNRQ EVGHKSCLGI DLNSNWGFKW KGQKKVRPCK
EGFPGREPFE AVETRAVADW LESKKAEGVI IKSFVDLHSY GQLCASIPSV SLARLMS
//
