ID A0A3N2PWQ7_9PEZI Unreviewed; 430 AA.
AC A0A3N2PWQ7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Zinc carboxypeptidase A {ECO:0000313|EMBL:ROT38951.1};
GN ORFNames=SODALDRAFT_332391 {ECO:0000313|EMBL:ROT38951.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT38951.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT38951.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT38951.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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; ML119054; ROT38951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2PWQ7; -.
DR STRING; 1314773.A0A3N2PWQ7; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000272025; 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:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 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; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ROT38951.1};
KW Hydrolase {ECO:0000313|EMBL:ROT38951.1};
KW Protease {ECO:0000313|EMBL:ROT38951.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017978008"
FT DOMAIN 177..199
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 430 AA; 47501 MW; 444AB6A3A14F79C3 CRC64;
MRVQSAITAL AVLVTTVAAE DRVSYDGYKV FRIDTHDNSE EIHRLIDGLH AVEVSCGESD
HFELAVAPED VEAFQALGLD ASLLSEDLSV DLELEGPVES FYESEESNYT IEVRQQALPA
LSWFSSYRPY ADHATFFSQM QAAFPQNSRI FNVGNSHQGR SIYGIHLWGP NGQGNRPAIY
FHGTVHAREW ISAPVVEYLT WQLINGYRNN DALVRSFFNK YDFYIVPFVN PDGFVHTQSS
DRLWRKNRQP RSGTSCVGTD GNRNWNFQWS TPGGASTSPC SETYRGQAAG DTPEIRALTT
FTNSLRTRGI KLFIDWHSYG QYILLPYGYN CQARAPNHNA QMSVAAGYSS AIRAVSGTRF
TYGPSCSTLY ATTGSSPDYM GGAMGAEYAW TVELRPGPGS GSSGFVLPAG QIAASGAEQW
EGIKYVLNTI
//
