ID J7RBN9_KAZNA Unreviewed; 939 AA.
AC J7RBN9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN Name=KNAG0J02240 {ECO:0000313|EMBL:CCK72305.1};
GN OrderedLocusNames=KNAG_0J02240 {ECO:0000313|EMBL:CCK72305.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK72305.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK72305.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000256|ARBA:ARBA00003273}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004128}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|ARBA:ARBA00010918, ECO:0000256|RuleBase:RU361240}.
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DR EMBL; HE978323; CCK72305.1; -; Genomic_DNA.
DR AlphaFoldDB; J7RBN9; -.
DR STRING; 1071383.J7RBN9; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; TPWPVTI; -.
DR OrthoDB; 277019at2759; -.
DR Proteomes; UP000006310; Chromosome 10.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03875; M28_Fxna_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR048024; Fxna-like_M28_dom.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF56; VACUOLAR MEMBRANE PROTEASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..321
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 544..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 106086 MW; 638441BB0111F406 CRC64;
MSILNTLRAT FRYRKTNVSI CILVAYSLVA LLYVSDQIRY KYPSPNDKSL IKTHLDKSWM
DLQNITFSYH PYTSRDNDRV HDYLLERIND IVETRPFATV SDDMADKSSS IFKQTDTFNA
SSTKSRVIYF ESSNVVVKLT GKNSQLPGLL LSAHFDSVPT SHGATDDGKG IVSLLALLDY
YSKNQPERTL VFNFNNDEEF GLLGATHFLN HKWSKLVNYF LNLEGAGTGS KSVLLRTSDI
STARIYRDAV KVEPFGNSIF QQGFNQRQIR SETDYKVYSA SGLRGWDIAF FKPRDLYHTG
NDDVKHTSKE ALWHMLHTSW QLTEYMNTFT EDANFNTSPA IYFDFAGLKF YACSAKSLFA
INCILLVLVP IVLIPFHTLT NSRHQLNEAG LLLWLRLPLT FIIAIGVLTV TELFLYDVNR
FVVFRDYISP LLMFASEFLL INIILLSVLE YFWPSRLMKD ITLLQLNFVV WGMLLYATYL
LRTTDYGTTG IYIVTMLFVS LSGALFIKYL ASLISPPGYK KTAVRDNSPD GSIVPAPMQT
ASANPAVNEQ PNNLEGRQNS VSVSDSGDDE RAPLLPFSSS RTEGTEILVP PASAAEGGLV
KDTQYEWIFQ FIILIPVLVL LFQNLVEVLS ALSQTVVESR TSMQLVWNTL FGGAVILCFT
TLPFLKVGFK MTAALLFVFA GLLVRTIILS PFTGEVPLKI RFSQNLNGNV EVTGVGSNLG
FLEDVLVDMP SVKQRAEQVH CSKETQTCSY QGLKSNLVNC DSQGEEQQMM SIEVLQNDHK
NENRSKYAPM NAEIKIHSKE NRACTLYFNN TFGSSSLVKE VTVYLNVNKT NSTKFRWHKG
IDELQLHKLD FGKEFYHIGI EWFPKIISGY ADAGTKPDED VLGIVAMCYW GEFDSTTMCN
GESRRMVPAY DELLEYSPIH YTFTNRDKGL VYGKQYVEL
//
