ID B5VNS6_YEAS6 Unreviewed; 1027 AA.
AC B5VNS6;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=YLR389Cp-like protein {ECO:0000313|EMBL:EDZ70415.1};
GN ORFNames=AWRI1631_124150 {ECO:0000313|EMBL:EDZ70415.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ70415.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ70415.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ70415.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDZ70415.1}.
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DR EMBL; ABSV01001693; EDZ70415.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VNS6; -.
DR MEROPS; M16.008; -.
DR Proteomes; UP000008988; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 86..221
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 248..426
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 432..712
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 716..898
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1027 AA; 117702 MW; 75F29043D3089F22 CRC64;
MGVSLLASSS AFVTKPLLTQ LVHFSPISLN FTVRRFKPFT CLSRYYTTNP YNMTSNFKTF
NLDFLKPDLD ERSYRFIELP NKLKALLIQD PKADKAAASL DVNIGAFEDP ENLPGLAHFC
EHLLFMGSEK FPDENEYSSY LSKHGGSSNA YTASQNTNYF FEVNHQHLFG ALDRFSGFFS
CPLFNKDSTD KEINAVNSEN KKNLQNDIWR IYQLDKSLTN TKHPYHKFST GNIEILGTLP
KENGLNVRDE LLKFHKNFYS ANLMKLCILG REDLDTLSNW TYDLFKDVAN NGREVPLYAE
PIMQPEHLQK IIQVRPVKDL KKLEISFTVP DMEEHWESKP PRILSHLIGH EGSGSLLAHL
KKLGWANELS AGGHTVSKGN AFFAVDIDLT DNGLTHYRDV IVLIFQYIEM LKNSLPQKWI
FNELQDISNA TFKFKQAGSP SSTVSSLAKC LEKDYIPVNR ILAMGLLTKY EPDLLTQYTD
ALVPENSRVT LISRSLETDS AEKWYGTAYK VVDYPADLIK NMKSPGLNPA LTLPRPNEFV
STNFKVHKID GIKPLDEPVL LLSDDVSKLW YKKDDRFWQP RGYIYLSFKL PHTHASIINS
MLSTLYTQLA NDALKDLQYD AACADLRISF NKTNQGLAIT ASGFNEKLII LLTRFLQGVN
SFEPKKDRFE ILKDKTIRHL KNLLYEVPYS QMSNYYNAII NERSWSTAEK LQVFEKLTFE
QLINFIPTIY EGVYFETLIH GNIKHEEALE VDSLIKSLIP NNIHNLQVSN NRLRSYLLPK
GKTFRYETAL KDSRNVNSCI QHVTQLDVYS EDLSALSGLF AQLIHEPCFD TLRTKEQLGY
VVFSSSLNNH GTANIRILIQ SEHTTPYLEW RINNFYETFG QVLRDMPEED FEKHKEALCN
SLLQKFKNMA EESARYTAAI YLGDYNFTHR QKKAKLVANI TKQQMIDFYE NYIMSENASK
LILHLKSQVE NKELNENELD TAKYPTGQLI EDVGAFKSTL FVAPVRQPMK DFEISAPPKL
NNSSESD
//