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Database: UniProt
Entry: H2AUU8_KAZAF
LinkDB: H2AUU8_KAZAF
Original site: H2AUU8_KAZAF 
ID   H2AUU8_KAZAF            Unreviewed;       488 AA.
AC   H2AUU8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   07-JUN-2017, entry version 32.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCF58148.1};
GN   Name=KAFR0D05010 {ECO:0000313|EMBL:CCF58148.1};
GN   ORFNames=KAFR_0D05010 {ECO:0000313|EMBL:CCF58148.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 /
OS   CECT 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces
OS   africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF58148.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF58148.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; HE650824; CCF58148.1; -; Genomic_DNA.
DR   RefSeq; XP_003957283.1; XM_003957234.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; CCF58148; CCF58148; KAFR_0D05010.
DR   GeneID; 13882550; -.
DR   KEGG; kaf:KAFR_0D05010; -.
DR   InParanoid; H2AUU8; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000005220; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:EnsemblFungi.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005220};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   488 AA;  54090 MW;  2C3D2C6950B3EB8A CRC64;
     MLRVHLREMS TAINYSNEFV SFLNASHSPY HAVENVRQHL LSHGFEELTE RGNWAGKVLH
     KGKYFVTRNN SSLIGFVVGN KWVPGNPIAI TGAHTDSPVL RIKPISKRTN EKYMQVGIEC
     YGGGIWHSWF DRDLGLAGRV FVNDKNSGKS ISKLVDINRP LLKIPSLAIH LDRSVNEKFQ
     FNKESQLLPV LGLANEDSCG NEKLKQESTE AFNSIKSIVE RHHEDLLKLV VKELSLESVN
     DIVDFELILY DHDAACLGGL NNEFVYSGRL DNLTSTFTSM HGLTLASETN IENEEGIRLI
     SMFDHEEIGS SSAQGADSNF LPNILERLTS LKCDGTDATD PSPRSLILET SAKSFFLSSD
     VAHAVHPNYA SKYESQHKPL IGQGPVIKIN ANQRYMTNSP GMVLLKKIAD KCEIPLQLFV
     VANDSSCGST IGPILASKTG IRTLDIGNPI LSMHSIRETG GALDIDYQIR LFKGFFESYS
     TLEGEIIV
//
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