ID G3BCD9_CANTC Unreviewed; 287 AA.
AC G3BCD9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Zincin {ECO:0000313|EMBL:EGV60813.1};
GN ORFNames=CANTEDRAFT_116877 {ECO:0000313|EMBL:EGV60813.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV60813.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; GL996528; EGV60813.1; -; Genomic_DNA.
DR RefSeq; XP_006690027.1; XM_006689964.1.
DR AlphaFoldDB; G3BCD9; -.
DR STRING; 590646.G3BCD9; -.
DR GeneID; 18248483; -.
DR KEGG; cten:CANTEDRAFT_116877; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_969765_0_0_1; -.
DR OrthoDB; 1981312at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF287; PROTEIN TMA108; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..170
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 287 AA; 33473 MW; 455871B25944BD90 CRC64;
MQDYLFKDDV LQTQQLVAHE LVHQWIGNLV SFDDWKYVWL NESFATFFGN HFVSIIDPSY
SFVEELIDMS GRMVRTGDVN IQKFMNGVRL TGDTTTGELF NHQVYEKGIL MLRMIGNILD
PNTIDNFEVF LASMSKFVEA HRFESIKASE IWQFFLQEFD IDLLTFVSMW IRYDKFPFIQ
VSQKNGELVI EQAQSKPYQF PLVVSTTERD YQFYIKDKTT KVKLDEQVVA VNKHRVALVK
QDISKKLVKD LEPHLGRLDA LSYLIDYPDS GSGVHQMLQG VLRKQTK
//
