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
//