ID D8PRX9_SCHCM Unreviewed; 508 AA.
AC D8PRX9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN ORFNames=SCHCODRAFT_64852 {ECO:0000313|EMBL:EFJ02561.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ02561.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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}.
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DR EMBL; GL377302; EFJ02561.1; -; Genomic_DNA.
DR RefSeq; XP_003037463.1; XM_003037417.1.
DR AlphaFoldDB; D8PRX9; -.
DR GeneID; 9585095; -.
DR KEGG; scm:SCHCO_02610501; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02610501; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_2_1; -.
DR InParanoid; D8PRX9; -.
DR OMA; HQHAREH; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000007431; 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 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..508
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120227"
FT DOMAIN 143..486
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
FT REGION 317..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 508 AA; 56509 MW; BC6C2E9FED1E8D4F CRC64;
MSARTIIWLV FAALAQVVHS EGLAYGEDQQ PLVSTPQTRA SVLYHLQPGA DGFAVHKIAD
VLEHANLDVW HLSPERGAYV YVRDAGEERT MEKILDRVNS AAVERTPISA PPPPPADHAY
PASAFPWNTS LSHLPNSTYH NTYHSYLELH DMLYALHDAY PDVVTIVEYG RSSEGRPLLG
AVIQDEEVPS DEEKLLSFSH AHSGGRKGEA DTKLAFVISG AQHSREWIAT STASYLAHAL
SSNTSEPGSL RSLLKHFDFH IIPTPNPDGY VYTWEHDRFW HKNRQPLGLG VECTGIDLNR
NWGYKWRPVT YGDVDLSSSD DNSWQGEADL KKKHKKPKPT PNPCSASFPG SRPFQAPEVN
ALANYVTAIG SGVGGAPGRE IGVYIDLRSF GQMLSTPYSF SCQRMPRDNE DQLEAAMGAV
KRMKAAHGMG YKTGRLCELL YNAGGNIMDY MYKRESIKYS YSLHLRDTGT YGFLIPPEWI
RPVGEETAQL VTYLAHFVAR QRQLPDAP
//