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Database: UniProt
Entry: I2H7V3_TETBL
LinkDB: I2H7V3_TETBL
Original site: I2H7V3_TETBL 
ID   I2H7V3_TETBL            Unreviewed;       609 AA.
AC   I2H7V3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   Name=TBLA0H01680 {ECO:0000313|EMBL:CCH62455.1};
GN   ORFNames=TBLA_0H01680 {ECO:0000313|EMBL:CCH62455.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62455.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH62455.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; HE806323; CCH62455.1; -; Genomic_DNA.
DR   RefSeq; XP_004181974.1; XM_004181926.1.
DR   AlphaFoldDB; I2H7V3; -.
DR   MEROPS; A01.A91; -.
DR   GeneID; 14497612; -.
DR   KEGG; tbl:TBLA_0H01680; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_023427_0_0_1; -.
DR   InParanoid; I2H7V3; -.
DR   OMA; GYPIVPL; -.
DR   OrthoDB; 1968535at2759; -.
DR   Proteomes; UP000002866; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..609
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003660560"
FT   TRANSMEM        591..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          65..453
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   609 AA;  66825 MW;  8C04A0BA15DDF495 CRC64;
     MYLLLNIILH TILLQSLRPV QSLLFEKDII NVLKKNSDLS DIERLAKLQF TEFPRLIIGK
     DLGTIYSNVS LGTPSQLQRL SIDIAQPYVW VRSGRNSTEC DKPGSFCVNY SEYYANASNT
     SRVLNNNYIQ NIFFVDGNAI SGATYSDRIL FPNMTYGNDD INIHRNSTRN FTLNATIDTH
     NLSVSNISFF DAYNYSSLRY GALGLGGGLV STNLGVTGPS DPFSLLNALL NSGVIQTASY
     SMWFANGSSY IDTKHFPYEE KKSDYGLIVF GGVDSSLIDG TFQSFTMIPY EDTSDGLTTS
     GYPILPMGPI YIIANSGRTL NLTTLDFLEP VLLDSRITNS RLPASFIIQV AIQLEAMYLE
     SLDRWVVPCS LADYNVNFDF SFGSVRIRVP LEDFLVPSGL TGDNKTIHFS QNEDACYLAM
     YPNTDIGFNI LGTPFLKNAV IAVDHSSSQI AIGKAISGKD IYSNNINSLI PSLSSSISSD
     STPSTVQAIA SGTIPFAITR NNSQYNSLTM RASKIGSEIP VFPGDFWGTV DSNGLVTIGR
     SFYETRQRST STSSSSLFAN LSFNSASQKT ASGAGTSLKP MKSFYPHKST PWAWISILMC
     SILFAIVIL
//
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