ID A0A074YT37_AURPU Unreviewed; 558 AA.
AC A0A074YT37;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative vacuolar carboxypeptidase Cps1 {ECO:0000313|EMBL:KEQ90006.1};
GN ORFNames=M438DRAFT_393815 {ECO:0000313|EMBL:KEQ90006.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ90006.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ90006.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ90006.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KL584974; KEQ90006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074YT37; -.
DR STRING; 1043002.A0A074YT37; -.
DR HOGENOM; CLU_021802_11_0_1; -.
DR OrthoDB; 3672990at2759; -.
DR Proteomes; UP000030706; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KEQ90006.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037217-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037217-2}.
FT DOMAIN 272..424
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ SEQUENCE 558 AA; 62165 MW; CFD35A5CA80B31F7 CRC64;
MVMGKCSRAF WRGPESASVR SVIGKKEAFN LPANGHPGNE KPEGDTKVNT WCPIAEPTAI
EDGLTSSTEF AKNKDLLKQQ VERLSAAVNV PSVSYDDNYE VDKDPRWHAF VTLHETLKSH
FPRVHEKMVL EKVHSYGLLH TMPGSSQDLK PLVIMAHLDV VPVPDPTRWK HPPFEAYFDG
QWLWGRGSVD CKNNLIGIYS AMERLLEQDF KSKRTIILSF GFDEETGGFR GAKYMAAHLK
EKYGENSMGM IIDEGGSGIR TIDGVAYALP AIAEKGFLDI VLTLNTPGGH SSAPPKNTNI
GITSRFITAV EEHPFGPHID EHNPFWGYLK CEVENSPKAS EPWLREALEK KEDFADRLID
SRGDKVRWSI QTSQSVDVVN GGIKDNQLPE TTETIINYRF LPSDKIDDVL KTVADVLAPL
ANNYSIAVQG PGYSQIDRGF GVLNISSSNI LQPSPLSPTG PDVGVWNIFA GTIRQVFENT
GEKLSAKKVV PVGTISTGNT DTAHYWQLTK NIYRFSPRWE GTSEGVHTVD ERIDMQAHLS
GLRFYYELIR NMDSFVDN
//
