ID M2NIJ3_BAUPA Unreviewed; 581 AA.
AC M2NIJ3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN ORFNames=BAUCODRAFT_31563 {ECO:0000313|EMBL:EMC99219.1};
OS Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS (Baudoinia compniacensis (strain UAMH 10762)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC99219.1, ECO:0000313|Proteomes:UP000011761};
RN [1] {ECO:0000313|EMBL:EMC99219.1, ECO:0000313|Proteomes:UP000011761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC99219.1,
RC ECO:0000313|Proteomes:UP000011761};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB445552; EMC99219.1; -; Genomic_DNA.
DR RefSeq; XP_007673602.1; XM_007675412.1.
DR AlphaFoldDB; M2NIJ3; -.
DR STRING; 717646.M2NIJ3; -.
DR GeneID; 19111517; -.
DR KEGG; bcom:BAUCODRAFT_31563; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; WFYHQLH; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000011761; Unassembled WGS sequence.
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 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; INACTIVE METALLOCARBOXYPEPTIDASE ECM14; 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; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Reference proteome {ECO:0000313|Proteomes:UP000011761};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..581
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004022138"
FT DOMAIN 389..399
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 581 AA; 65260 MW; B160DEE3068B4EF2 CRC64;
MHLTLASLLA LPFGLLQVVL AVPAPADYAQ QHPLDVAALP KQATWKRLSD RIIESIWKDG
AHETDKDLPD PFAFRGYDRE VVIRFNVSTA EEARSLAEAS ETLLLDIWGF SQEWVDIRIP
KDIVKPMLGL LPSSLQRSYI PLLRERELSE AVRATYLTAR NRGPAIKAKD SLDSGSHIHI
DQMDKVGATE EDLFFSQYRP LSVLHPWMRF LASIYPGHVQ KINIGISAQG RGIPALRVGN
SKRPNRETVL IVGGLHAREW ISTSTVSYVA YHFVTCYGNS ARITALMDQL DFVFVPTLNP
DGYAYTWETD RLWRKNRQRT GLRFCQGIDL DRAFSFQWDG DSTTSGNPCS ESFAGEQPFE
AVEAKALADW AKNETTHNNV TFVGFLDMHS YAQEILYPYS FSCDEKPPGL ENLEELAIGI
EKAIRSTHGH KYEIMPACEG NVAVNNGFRQ SLSPRMEASG GSILDWFYHE MHVRYAYQLK
LRDKGLYGFL LPAENIIPTG EEILEAVLYF AEFLGDVYGS GMDVKESTAN GKVQNDQGVP
KDKDFAFSAD DIGDDWVVID GQAELSMSDL MLSESLRQRQ D
//
